The analysis of biological samples with polarized infrared spectroscopy (p-IR) has long been a widely practiced method for the determination of sample orientation and structural properties. In contrast to earlier works, which employed this method to investigate the fundamental chemistry of biological systems, recent interests are moving toward “real-world” applications for the evaluation and diagnosis of pathological states. This focal point review provides an up-to-date synopsis of the knowledge of biological materials garnered through linearly p-IR on biomolecules, cells, and tissues. An overview of the theory with special consideration to biological samples is provided. Different modalities which can be employed along with their capabilities and limitations are outlined. Furthermore, an in-depth discussion of factors regarding sample preparation, sample properties, and instrumentation, which can affect p-IR analysis is provided. Additionally, attention is drawn to the potential impacts of analysis of biological samples with inherently polarized light sources, such as synchrotron light and quantum cascade lasers. The vast applications of p-IR for the determination of the structure and orientation of biological samples are given. In conclusion, with considerations to emerging instrumentation, findings by other techniques, and the shift of focus toward clinical applications, we speculate on the future directions of this methodology.
PhamM.C.MoslihJ.LacazeP.C.. “Investigation by In-Situ IR Analysis (MIR-FT-IRS Method) of the Polymer-Chain Orientation of Films Electrochemically Deposited on Iron”. Bull. Soc. Chim. Fr. 1990. (1): 32–37.
2.
MillerP.J.JacksonJ.F.PorterR.S.. “Infrared Dichroism of Polyethylene Crystallized by Orientation and Pressure in a Capillary Viscometer”. J. Polym. Sci., Part B: Polym. Phys. 1973. 11(10): 2001–2012.
3.
PézoletM.PellerinC.Prud'hommeR.E.BuffeteauT.. “Study of Polymer Orientation and Relaxation by Polarization Modulation and 2D-FT-IR Spectroscopy”. Vib. Spectrosc. 1998. 18(2): 103–110.
4.
RamakrishnanN.XiaY.BidthanapallyA.LuM.. “Determination of Zonal Boundaries in Articular Cartilage Using Infrared Dichroism”. Appl. Spectrosc. 2007. 61(12): 1404–1409.
5.
BakirG.GirouardB.E.WiensR.MastelS., et al. “Orientation Matters: Polarization Dependent IR Spectroscopy of Collagen From Intact Tendon Down to the Single Fibril Level”. Molecules. 2020. 25(18): 4295.
6.
KoziolP.LiberdaD.KwiatekW.M.WrobelT.P.. “Macromolecular Orientation in Biological Tissues Using a Four-Polarization Method in FT-IR Imaging”. Anal. Chem. 2020. 92(19): 13313–13318.
7.
BiX.LiG.DotyS.B.CamachoN.P.. “A Novel Method for Determination of Collagen Orientation in Cartilage by Fourier Transform Infrared Imaging Spectroscopy (FT-IRIS)”. Osteoarthr. Cartil. 2005. 13(12): 1050–1058.
8.
CamachoN.P.RinnerthalerS.PaschalisE.P.MendelsohnR., et al. “Complementary Information on Bone Ultrastructure From Scanning Small Angle X-Ray Scattering and Fourier-Transform Infrared Microspectroscopy”. Bone. 1999. 25(3): 287–293.
9.
WilsonR.H.SmithA.C.KacurakovaM.SaundersP.K., et al. “The Mechanical Properties and Molecular Dynamics of Plant Cell Wall Polysaccharides Studied by Fourier-Transform Infrared Spectroscopy”. Plant Physiol. 2000. 124(1): 397–405.
10.
BinderH.. “The Molecular Architecture of Lipid Membranes: New Insights From Hydration-Tuning Infrared Linear Dichroism Spectroscopy”. Appl. Spectrosc. Rev. 2003. 38(1): 15–69.
11.
ViganoC.ManciuL.BuyseF.GoormaghtighE.RuysschaertJ.M.. “Attenuated Total Reflection IR Spectroscopy as a Tool to Investigate the Structure, Orientation and Tertiary Structure Changes in Peptides and Membrane Proteins”. Biopolymers. 2000. 55(5): 373–380.
12.
WaeytensJ.MathurinJ.Deniset-BesseauA.ArluisonV., et al. “Probing Amyloid Fibril Secondary Structures by Infrared Nanospectroscopy: Experimental and Theoretical Considerations”. Analyst. 2021. 146(1): 132–145.
13.
BradburyE.M.PriceW.C.WilkinsonG.R.. “Infrared Studies of Molecular Configurations of DNA”. J. Mol. Biol. 1961. 3(3): 301–317.
14.
FranklinR.E.GoslingR.G.. “Molecular Configuration in Sodium Thymonucleate”. Nature. 1953. 171(4356): 740–741.
15.
FraserM.J.FraserR.D.B.. “Evidence on the Structure of Deoxyribonucleic Acid from Measurements with Polarized Infra-Red Radiation”. Nature. 1951. 167(4254): 761–762.
16.
FritzscheH.LangH.PohleW.. “Evidence for B–C Transition in Ultaviolet-Irradiated DNA—An Infrared Linear Dichroism Study”. Biochim. Biophys. Acta. 1976. 432(3): 409–412.
17.
PohleW.FritzscheH.ZhurkinV.B.IvanovV.I.. “The DNA Backbone Geometry as Obtained by Infrared Linear Dichroism and Conformational Analysis”. Stud. Biophys. 1980. 79: 73–74.
18.
FritzscheH.. “Infrared Spectroscopy and Infrared Linear Dichroism of Nucleic Acids”. J. Mol. Struct. 1991. 242: 245–261.
19.
AmbroseE.J.ElliottA.TempleR.B.. “New Evidence on the Structure of Some Proteins From Measurements With Polarized Infra-Red Radiation”. Nature. 1949. 163(4153): 859–862.
20.
AmbroseE.J.ElliottA.WilsonA.H.. “The Structure of Synthetic Polypeptides. II. Investigation with Polarized Infra-Red Spectroscopy”. Proc. R. Soc. London, Ser. A. 1951. 205(1080): 47–60.
21.
Kimura-SudaH.NakamuraF.OsetoR.KanehiraY., et al. “Relationships Among Collagen Fiber Orientation, Mineralization, Mineral Maturity, and Crystallinity”. Mol. Cryst. Liq. Cryst. 2020. 707(1): 154–160.
22.
WiensR.FindlayC.R.BaldwinS.G.KreplakL., et al. “High Spatial Resolution (1.1mm and 20nm) FT-IR Polarization Contrast Imaging Reveals Pre-Rupture Disorder in Damaged Tendon”. Faraday Discuss. 2016. 187(0): 555–573.
23.
Eklouh-MolinierC.HappillonT.BoulandN.FichelC., et al. “Investigating the Relationship Between Changes in Collagen Fiber Orientation During Skin Aging and Collagen/Water Interactions by Polarized-FT-IR Microimaging”. Analyst. 2015. 140(18): 6260–6268.
24.
ChrabaszczK.KaminskaK.SongC.L.MorikawaJ., et al. “Fourier Transform Infrared Polarization Contrast Imaging Recognizes Proteins Degradation in Lungs Upon Metastasis From Breast Cancer”. Cancers. 2021. 13(2): 162.
25.
HikimaY.MorikawaJ.HashimotoT.. “FT-IR Image Processing Algorithms for In-Plane Orientation Function and Azimuth Angle of Uniaxially Drawn Polyethylene Composite Film”. Macromolecules. 2011. 44(10): 3950–3957.
26.
KosowskaK.KoziołP.LiberdaD.WrobelT.. “Spatially Resolved Macromolecular Orientation in Biological Tissues Using FT-IR Imaging”. Clinical Spectroscopy. 2021. 3: 100013.
27.
XiaY.RamakrishnanN.BidthanapallyA.. “The Depth-Dependent Anisotropy of Articular Cartilage by Fourier-Transform Infrared Imaging (FT-IRI)”. Osteoarthr. Cartil. 2007. 15(7): 780–788.
28.
GoormaghtighE.RuysschaertJ.-M.. “Polarized Attenuated Total Reflection Infrared Spectroscopy as a Tool to Investigate the Conformation and Orientation of Membrane Components”. In: BrasseurR., editor. Molecular Description of Biological Membrane Components by Computer Aided Conformational Analysis. Milton, UK: Taylor and Francis Group, 2019. Chapter 1.B.3, Pp. 285–330.
29.
QuaroniL.ZlatevaT.BedollaD.MassaroS.TorreV.. “Measurement of Molecular Orientation in a Subcellular Compartment by Synchrotron Infrared Spectromicroscopy”. ChemPhysChem. 2008. 9(10): 1380–1382.
30.
XiaY.MittelstaedtD.RamakrishnanN.SzarkoM.BidthanapallyA.. “Depth-Dependent Anisotropies of Amides and Sugar in Perpendicular and Parallel Sections of Articular Cartilage by Fourier Transform Infrared Imaging”. Microsc. Res. Tech. 2011. 74(2): 122–132.
31.
HinrichsK.ShaykhutdinovT.. “Polarization-Dependent Atomic Force Microscopy-Infrared Spectroscopy (AFM-IR): Infrared Nanopolarimetric Analysis of Structure and Anisotropy of Thin Films and Surfaces”. Appl. Spectrosc. 2018. 72(6): 817–832.
32.
BadenN.KobayashiH.UrayamaN.. “Submicron-Resolution Polymer Orientation Mapping by Optical Photothermal Infrared Spectroscopy”. Int. J. Polym. Anal. Charact. 2020. 25(1): 1–7.
33.
GiubertoniG.CaporalettiF.RoetersS.J.ChatterleyA.S., et al. “In Situ Identification of Secondary Structures in Unpurified Bombyx mori Silk Fibrils Using Polarized Two-Dimensional Infrared Spectroscopy”. Biomacromolecules. 2022. 23(12): 5340–5349.
34.
HinrichsK.BlevinsB.FurchnerA.YadavalliN.S., et al. “Mid-Infrared Dual-Comb Polarimetry of Anisotropic Samples”. Nat. Sci. 2023. 3(2): E20220056.
35.
HinrichsK.SilaghiS.D.CobetC.EsserN.ZahnD.R.T.. “Ellipsometry from Infrared to Vacuum Ultraviolet: Structural Properties of Thin Anisotropic Guanine Films on Silicon”. Phys. Status Solidi B. 2005. 242(13): 2681–2687.
36.
RogersD.M.JasimS.B.DyerN.T.AuvrayF., et al. “Electronic Circular Dichroism Spectroscopy of Proteins”. Chem. 2019. 5(11): 2751–2774.
37.
AghighA.BancelinS.RivardM.PinsardM., et al. “Second Harmonic Generation Microscopy: A Powerful Tool for Bio-Imaging”. Biophys. Rev. 2023. 15(1): 43–70.
38.
CisekR.JosephA.HarveyM.TokarzD.. “Polarization-Sensitive Second Harmonic Generation Microscopy for Investigations of Diseased Collagenous Tissues”. Front. Physics. 2021. 9: 1–9.
39.
JamesonD.M.RossJ.A.. “Fluorescence Polarization/Anisotropy in Diagnostics and Imaging”. Chem. Rev. 2010. 110(5): 2685–2708.
40.
SchrofS.VargaP.GalvisL.RaumK.MasicA.. “3D Raman Mapping of the Collagen Fibril Orientation in Human Osteonal Lamellae”. J. Struct. Biol. 2014. 187(3): 266–275.
41.
CailleJ.P.PigeongosselinM.DousseauF.PezoletM.. “Orientation of the Contractile Proteins of Muscle-Fibers by Raman and Infrared Spectroscopy”. Biophys. J. 1987. 51(2): A279–A279.
42.
MasicA.BertinettiL.SchuetzR.GalvisL., et al. “Observations of Multiscale, Stress-Induced Changes of Collagen Orientation in Tendon by Polarized Raman Spectroscopy”. Biomacromolecules. 2011. 12(11): 3989–3996.
IwamotoH.. “Synchrotron Radiation X-ray Diffraction Studies on Muscle: Past, Present, and Future”. Biophys. Rev. 2019. 11(4): 547–558.
45.
RuprechtJ.NieldJ.. “Determining the Structure of Biological Macromolecules by Transmission Electron Microscopy, Single Particle Analysis and 3D Reconstruction”. Prog. Biophys. Mol. Biol. 2001. 75(3): 121–164.
46.
GräwertT.W.SvergunD.I.. “Structural Modeling Using Solution Small-Angle X-ray Scattering (SAXS)”. J. Mol. Biol. 2020. 432(9): 3078–3092.
47.
AnknerJ.F.HellerW.T.HerwigK.W.MeilleurF.MylesD.A.A.. “Neutron Scattering Techniques and Applications in Structural Biology”. Curr. Protoc. Protein Sci. 2013. 72(1): 1–34.
48.
HeC.HeH.ChangJ.ChenB., et al. “Polarisation Optics for Biomedical and Clinical Applications: A Review”. Light: Sci. Appl. 2021. 10(1): 194.
49.
HémonnotC.Y.J.KösterS.. “Imaging of Biological Materials and Cells by X-ray Scattering and Diffraction”. ACS Nano. 2017. 11(9): 8542–8559.
50.
ButlerH.J.AshtonL.BirdB.CinqueG., et al. “Using Raman Spectroscopy to Characterize Biological Materials”. Nat. Protoc. 2016. 11(4): 664–687.
BokobzaL.. “Infrared Linear Dichroism for the Analysis of Molecular Orientation in Polymers and in Polymer Composites”. Polymers. 2022. 14(6): 1257.
53.
BuffeteauT.PézoletM.. “Linear Dichroism in Infrared Spectroscopy”. In: ChalmersJ.M.GriffithsP.R., editors. Handbook of Vibrational Spectroscopy. Hoboken, NJ: John Wiley and Sons, Ltd, 2006. Pp. 693–710.
54.
FraserR.D.B.. “The Interpretation of Infrared Dichroism in Fibrous Protein Structures”. J. Chem. Phys. 1953. 21(9): 1511–1515.
55.
KafleK.ParkY.B.LeeC.M.StapletonJ.J., et al. “Effects of Mechanical Stretching on Average Orientation of Cellulose and Pectin in Onion Epidermis Cell Wall: A Polarized FT-IR Study”. Cellulose. 2017. 24(8): 3145–3154.
56.
Rodriguez-PerezJ.C.HamleyI.W.SquiresA.M.. “Infrared Linear Dichroism Spectroscopy on Amyloid Fibrils Aligned by Molecular Combing”. Biomacromolecules. 2011. 12(5): 1810–1821.
57.
ZhaoY.ZhuY.K.LuY.F.ShangL.W., et al. “Anisotropy of Bovine Nasal Cartilage Measured by Fourier Transform Infrared Imaging”. Appl. Phys. B: Lasers Opt. 2019. 125(12): 1–7.
58.
RamakrishnanN.XiaY.BidthanapallyA.. “Polarized IR Microscopic Imaging of Articular Cartilage”. Phys. Med. Biol. 2007. 52(15): 4601–4614.
59.
GregoriouV.G.TzavalasS.BollasS.T.. “Angular Dependence in Infrared Linear Dichroism: A Reevaluation of the Theory”. Appl. Spectrosc. 2004. 58(6): 655–661.
60.
MayerhöferT.G.. “Employing Theories Far Beyond Their Limits—Linear Dichroism Theory”. ChemPhysChem. 2018. 19(17): 2123–2130.
61.
HikimaY.MorikawaJ.HashimotoT.. “Wavenumber Dependence of FT-IR Image of Molecular Orientation in Banded Spherulites of Poly(3-Hydroxybutyrate) and Poly(L-Lactic Acid)”. Macromolecules. 2013. 46(4): 1582–1590.
62.
XuS.RowletteJ.LeeY.J.. “Imaging 3D Molecular Orientation by Orthogonal-Pair Polarization IR Microscopy”. Opt. Express. 2022. 30(6): 8436–8447.
63.
KangH.S.JohnsonW.C.. “Infrared Linear Dichroism Reveals That A-, B-, and C-DNAs in Films Have Bases Highly Inclined from Perpendicular to the Helix Axis”. Biochemistry. 1994. 33(27): 8330–8338.
64.
CamachoN.P.WestP.TorzilliP.A.MendelsohnR.. “FT-IR Microscopic Imaging of Collagen and Proteoglycan in Bovine Cartilage”. Biopolymers. 2001. 62(1): 1–8.
65.
VidalB.D.C.. “Using the FT-IR Linear Dichroism Method for Molecular Order Determination of Tendon Collagen Bundles and Nylon 6”. Acta Histochem. 2013. 115(7): 686–691.
66.
GadaletaS.J.CamachoN.P.MendelsohnR.BoskeyA.L.. “Fourier Transform Infrared Microscopy of Calcified Turkey Leg Tendon”. Calcif. Tissue Int. 1996. 58(1): 17–23.
67.
Sophia FoxA.J.BediA.RodeoS.A.. “The Basic Science of Articular Cartilage: Structure, Composition, and Function”. Sports Health. 2009. 1(6): 461–468.
68.
BiX.H.YangX.BostromM.P.G.CamachoN.P.. “Fourier Transform Infrared Imaging Spectroscopy Investigations in the Pathogenesis and Repair of Cartilage”. Biochim. Biophys. Acta. 2006. 1758(7): 934–941.
69.
BiX.H.YangX.BostromM.P.G.BartusikD., et al. “Fourier Transform Infrared Imaging and MR Microscopy Studies Detect Compositional and Structural Changes in Cartilage in a Rabbit Model of Osteoarthritis”. Anal. Bioanal. Chem. 2007. 387(5): 1601–1612.
70.
YinJ.H.XiaY.RamakrishnanN.. “Depth-Dependent Anisotropy of Proteoglycan in Articular Cartilage by Fourier Transform Infrared Imaging”. Vib. Spectrosc. 2011. 57(2): 338–341.
71.
AtkinsonG.A.ErnstJ.D.. “High-Sensitivity Analysis of Polarization by Surface Reflection”. Mach. Vis. Appl. 2018. 29(7): 1171–1189.
72.
RyuM.BalčytisA.WangX.VongsvivutJ., et al. “Orientational Mapping Augmented Sub-Wavelength Hyper-Spectral Imaging of Silk”. Sci. Rep. 2017. 7(1): 7419.
73.
MankarR.GajjelaC.C.Bueso-RamosC.E.YinC.C., et al. “Polarization Sensitive Photothermal Mid-Infrared Spectroscopic Imaging of Human Bone Marrow Tissue”. Appl. Spectrosc. 2022. 76(4): 508–518.
74.
YamunaP.KevinY.RohitB.. “Polarimetric Infrared Spectroscopic Imaging Using Quantum Cascade Lasers”. Proc. SPIE. 2020. 11252: 1125210
75.
NabedrykE.BretonJ.. “Orientation of Intrinsic Proteins in Photosynthetic Membranes–Polarised Infrared Spectroscopy of Chloroplast and Chromatophores”. Biochim. Biophys. Acta. 1981. 635(3): 515–524.
76.
LeeY.J.. “Concurrent Polarization IR Analysis to Determine the 3D Angles and the Order Parameter for Molecular Orientation Imaging”. Opt. Express. 2018. 26(19): 24577–24590.
77.
KoziolP.KosowskaK.LiberdaD.BorondicsF.WrobelT.P.. “Super-Resolved 3D Mapping of Molecular Orientation Using Vibrational Techniques”. J. Am. Chem. Soc. 2022. 144(31): 14278–14287.
78.
MilaniS.BombelliF.B.BertiD.HaussT., et al. “Structural Investigation of Bilayers Formed by 1-Palmitoyl-2-Oleoylphosphatidylnucleosides”. Biophys. J. 2006. 90(4): 1260–1269.
79.
GoormaghtighE.RaussensV.RuysschaertJ.-M.. “Attenuated Total Reflection Infrared Spectroscopy of Proteins and Lipids in Biological Membranes”. Biochim. Biophys. Acta. 1999. 1422(2): 105–185.
80.
MilosevicM.. “Orientation Studies and ATR Spectroscopy”. In: VithaM.F.MilosevicM., editors. Internal Reflection and ATR Spectroscopy. Hoboken, NJ: John Wiley and Sons, Ltd, 2012. Chapter 21, Pp. 214–219.
81.
RyuM.NgS.H.AnandV.LundgaardS., et al. “Attenuated Total Reflection at THz Wavelengths: Prospective Use of Total Internal Reflection and Polariscopy”. Appl. Sci. 2021. 11(16): 7632.
82.
RyuM.NgS.H.HanM.AnandV., et al. “Polariscopy with Optical Near-Fields”. Nanoscale Horiz. 2022. 7(9): 1047–1053.
83.
GassnerC.AdegokeJ.A.PatelS.K.SharmaV.J., et al. “Improved Tissue Preparation for Multimodal Vibrational Imaging of Biological Tissues”. Clinical Spectroscopy. 2022. 4: 100021.
84.
FaoláinE. ÓHunterM.B.ByrneJ.M.KelehanP., et al. “A Study Examining the Effects of Tissue Processing on Human Tissue Sections Using Vibrational Spectroscopy”. Vib. Spectrosc. 2005. 38(1): 121–127.
85.
ZohdiV.WhelanD.R.WoodB.R.PearsonJ.T., et al. “Importance of Tissue Preparation Methods in FT-IR Micro-Spectroscopical Analysis of Biological Tissues: ‘Traps for New Users’”. PLoS One. 2015. 10(2): E0116491.
86.
HughesC.GauntL.BrownM.ClarkeN.W.GardnerP.. “Assessment of Paraffin Removal from Prostate FFPE Sections Using Transmission Mode FT-IR-FPA Imaging”. Anal. Methods. 2014. 6(4): 1028–1035.
87.
WuY.C.ZhangX.X.MaoZ.H.YinJ.H.. “Study on the Anisotropy of Collagenous Fibers in Articular with Infrared Imaging”. Guangpuxue Yu Guangpu Fenxi [Spectrosc. Spectr. Anal.]. 2016. 36(7): 2071–2075.
88.
ThavarajahR.MudimbaimannarV.K.ElizabethJ.RaoU.K.RanganathanK.. “Chemical and Physical Basics of Routine Formaldehyde Fixation”. Int. J. Oral Maxillofac. Pathol. 2012. 16(3): 400–405.
89.
De VitoG.ParlantiP.CecchiR.LuinS., et al. “Effects of Fixatives on Myelin Molecular Order Probed with RP-CARS Microscopy”. Appl. Opt. 2020. 59(6): 1756–1762.
90.
SmithsonK.G.MacvicarB.A.HattonG.I.. “Polyethylene Glycol Embedding: A Technique Compatible with Immunocytochemistry, Enzyme Histochemistry, Histofluorescence and Intracellular Staining”. J. Neurosci. Methods. 1983. 7(1): 27–41.
De AguiarH.B.GiganS.BrasseletS.. “Polarization Recovery Through Scattering Media”. Sci. Adv. 2017. 3(9): E1600743.
93.
LaydenD.GhoshN.VitkinA.. “Quantitative Polarimetry for Tissue Characterization and Diagnosis”. In: WangR.K.TuchinV.V., editors. Advanced Biophotonics: Tissue Optical Sectioning. Boca Raton: CRC Press, 2013. Chapter 2, P. 733.
94.
RyuM.HondaR.BalčytisA.VongsvivutJ., et al. “Hyperspectral Mapping of Anisotropy”. Nanoscale Horiz. 2019. 4(6): 1443–1449.
95.
WhittakerP.KlonerR.A.BoughnerD.R.PickeringJ.G.. “Quantitative Assessment of Myocardial Collagen With Picrosirius Red Staining and Circularly-Polarized Light”. Basic Res. Cardiol. 1994. 89(5): 397–410.
96.
WangW.H.MengL.HackettR.J.OdenbourgR.KeefeD.L.. “Limited Recovery of Meiotic Spindles in Living Human Oocytes After Cooling-Rewarming Observed Using Polarized Light Microscopy”. Hum. Reprod. 2001. 16(11): 2374–2378.
97.
NieminenM.T.RieppoJ.ToyrasJ.HakumakiJ.M., et al. “T-2 Relaxation Reveals Spatial Collagen Architecture in Articular Cartilage: A Comparative Quantitative MRI and Polarized Light Microscopic Study”. Magn. Reson. Med. 2001. 46(3): 487–493.
98.
JinL.W.ClabornK.A.KurimotoM.GedayM.A., et al. “Imaging Linear Birefringence and Dichroism in Cerebral Amyloid Pathologies”. Proc. Natl. Acad. Sci. U.S.A. 2003. 100(26): 15294–15298.
99.
RyuM.NishijimaY.MorimotoS.ToN., et al. “Hyperspectral Molecular Orientation Mapping in Metamaterials”. Appl. Sci. 2021. 11(4): 1544.
100.
RomeoM.DiemM.. “Correction of Dispersive Line Shape Artifact Observed in Diffuse Reflection Infrared Spectroscopy and Absorption/Reflection (Transflection) Infrared Micro-Spectroscopy”. Vib. Spectrosc. 2005. 38(1): 129–132.
101.
MillerL.M.DumasP.. “Chemical Imaging of Biological Tissue With Synchrotron Infrared Light”. Biochim. Biophys. Acta. 2006. 1758(7): 846–857.
JanassekP.HartmannS.MolitorA.MichelF.ElsäßerW.. “Investigations of the Polarization Behavior of Quantum Cascade Lasers by Stokes Parameters”. Opt. Lett. 2016. 41(2): 305–308.
104.
DumasP.MillerL.M.TobinM.J.. “Challenges in Biology and Medicine with Synchrotron Infrared Light”. Acta Phys. Pol. A. 2009. 115(2): 446–454.
105.
SantoroG.YousefI.JammeF.DumasP.EllisG.. “Infrared Synchrotron Radiation from Bending Magnet and Edge Radiation Sources for the Study of Orientation and Conformation in Anisotropic Materials”. Rev. Sci. Instrum. 2011. 82(3): 033710.
106.
KrizhanovskiiD.N.SanvittoD.CeccarelliS.SkolnickM.S.RobertsJ.S.. “Polarisation Properties of Optical Parametric Oscillator Emission in a Semiconductor Microcavity”. Phys. Status Solidi A. 2005. 202(14): 2621–2625.
107.
BeasleyJ.D.PhilipD.M.. “Achromatic Wave Plates for the Mid-Infrared”. Proc. SPIE. 2012. 8364: 83640I
108.
Viguet-CarrinS.GarneroP.DelmasP.D.. “The Role of Collagen in Bone Strength”. Osteoporosis Int. 2006. 17(3): 319–336.
109.
RichardsonW.J.HolmesJ.W.. “Emergence of Collagen Orientation Heterogeneity in Healing Infarcts and an Agent-Based Model”. Biophys. J. 2016. 110(10): 2266–2277.
110.
SmithaB.DonoghueM.. “Clinical and Histopathological Evaluation of Collagen Fiber Orientation in Patients with Oral Submucous Fibrosis”. Int. J. Oral Maxillofac. Pathol. 2011. 15(2): 154–160.
111.
LiH.BeraK.ToroP.FuP., et al. “Collagen Fiber Orientation Disorder from H&E Images is Prognostic for Early-Stage Breast Cancer: Clinical Trial Validation”. Npj Breast Cancer. 2021. 7(1): 104.
112.
NicolasJ.-D.KhanA.MarkusA.MohamedB.A., et al. “X-ray Diffraction and Second Harmonic Imaging Reveal New Insights into Structural Alterations Caused by Pressure-Overload in Murine Hearts”. Sci. Rep. 2020. 10(1): 19317.
113.
CarrJ.K.ZabugaA.V.RoyS.RizzoT.R.SkinnerJ.L.. “Assessment of Amide I Spectroscopic Maps for a Gas-Phase Peptide Using IR-UV Double-Resonance Spectroscopy and Density Functional Theory Calculations”. J. Chem. Phys. 2014. 140(22): 224111.
114.
BaronioC.M.BarthA.. “The Amide I Spectrum of Proteins: Optimization of Transition Dipole Coupling Parameters Using Density Functional Theory Calculations”. J. Phys. Chem. B. 2020. 124(9): 1703–1714.
115.
Michel-VillazM.SaibilH.R.ChabreM.. “Orientation of Rhodopsin Alpha-Helices in In Retinal Rod Outer Segment Membranes Studied by Infrared Linear Dichroism”. Proc. Natl. Acad. Sci. U.S.A. 1979. 76(9): 4405–4408.
116.
LudlamC.F.C.ArkinI.T.LiuX.M.RothmanM.S., et al. “Fourier Transform Infrared Spectroscopy and Site-Directed Isotope Labeling as a Probe of Local Secondary Structure in the Transmembrane Domain of Phospholamban”. Biophys. J. 1996. 70(4): 1728–1736.
117.
RaussensV.RuysschaertJ.M.GoormaghtighE.. “Fourier Transform Infrared Spectroscopy Study of the Secondary Structure of the Gastric H+,K+-ATpase and of its Membrane-Associated Proteolytic Peptides”. J. Biol. Chem. 1997. 272(1): 262–270.
118.
MarshD.PáliT.. “Infrared Dichroism from the X-ray Structure of Bacteriorhodopsin”. Biophys. J. 2001. 80(1): 305–312.
119.
MarshD.MüllerM.SchmittF.-J.. “Orientation of the Infrared Transition Moments for an Α-Helix”. Biophys. J. 2000. 78(5): 2499–2510.
FitterJ.LechnerR.E.BuldtG.DencherN.A.. “Internal Molecular Motions of Bacteriorhodopsin: Hydration-Induced Flexibility Studied by Quasielastic Incoherent Neutron Scattering Using Oriented Purple Membranes”. Proc. Natl. Acad. Sci. U.S.A. 1996. 93(15): 7600–7605.
122.
BechingerB.RuysschaertJ.-M.GoormaghtighE.. “Membrane Helix Orientation from Linear Dichroism of Infrared Attenuated Total Reflection Spectra”. Biophys. J. 1999. 76(1): 552–563.
123.
DiakovaG.GoddardY.A.KorbJ.-P.BryantR.G.. “Changes in Protein Structure and Dynamics as a Function of Hydration from 1H Second Moments”. J. Magn. Reson. 2007. 189(2): 166–172.
124.
BoykenS.E.BenhaimM.A.BuschF.JiaM., et al. “De Novo Design of Tunable, pH-Driven Conformational Changes”. Science. 2019. 364(6441): 658–664.
125.
Di RussoN.V.EstrinD.A.MartíM.A.RoitbergA.E.. “pH-Dependent Conformational Changes in Proteins and Their Effect on Experimental PKas: The Case of Nitrophorin 4”. PLoS Comput. Biol. 2012. 8(11): E1002761.
126.
MarshD.. “Dichroic Ratios in Polarized Fourier Transform Infrared for Nonaxial Symmetry of Beta-Sheet Structures”. Biophys. J. 1997. 72(6): 2710–2718.
127.
AmbroseE.J.ElliottA.WilsonA.H.. “Infra-Red Spectra and Structure of Fibrous Proteins”. Proc. R. Soc. London, Ser. A. 1951. 206(1085): 206–219.
128.
UchidaK.HaradaI.NakauchiY.MaruyamaK.. “Structural Properties of Connectin Studied by Ultraviolet Resonance Raman Spectroscopy and Infrared Dichroism”. FEBS Lett. 1991. 295(1–3): 35–38.
129.
NakauchiY.ToyamaA.HaradaI.MaruyamaK.. “Infrared Dichroism of an Elastic Portion (1200 kDa Fragment) of Connectin”. Proc. Jpn. Acad., Ser. B. 1993. 69(8): 224–226.
130.
LabeitS.GautelM.LakeyA.TrinickJ.. “Towards a Molecular Understanding of Titin”. Embo J. 1992. 11(5): 1711–1716.
131.
BangM.-L.CentnerT.FornoffF.GeachA.J., et al. “The Complete Gene Sequence of Titin, Expression of an Unusual ≈700 kDa Titin Isoform, Its Interaction with Obscurin Identify a Novel Z-Line to I-Band Linking System”. Circ. Res. 2001. 89(11): 1065–1072.
132.
WatanabeK.NairP.LabeitD.KellermayerM.S.Z., et al. “Molecular Mechanics of Cardiac Titin's PEVK and N2B Spring Elements”. J. Biol. Chem. 2002. 277(13): 11549–11558.
133.
HigashiS.KasaiM.OosawaF.WadaA.. “Ultraviolet Dichroism of F-Actin Oriented by Flow”. J. Mol. Biol. 1963. 7(4): 421–430.
134.
NealonJ.O.PhilominaL.S.McGuffinL.J.. “Predictive and Experimental Approaches for Elucidating Protein-Protein Interactions and Quaternary Structures”. Int. J. Mol. Sci. 2017. 18(12): 2623.
135.
Rodriguez-PerezJ.C.HamleyI.W.GrasS.L.SquiresA.M.. “Local Orientational Disorder in Peptide Fibrils Probed by a Combination of Residue-Specific C-13-O-18 Labelling, Polarised Infrared Spectroscopy and Molecular Combing”. Chem. Comm. 2012. 48(97): 11835–11837.
136.
BlankenfeldtW.ThomäN.H.WrayJ.S.GautelM.SchlichtingI.. “Crystal Structures of Human Cardiac Β-Myosin II S2-Δ Provide Insight into the Functional Role of the S2 Subfragment”. Proc. Natl. Acad. Sci. U.S.A. 2006. 103(47): 17713–17717.
137.
BellaJ.EatonM.BrodskyB.BermanH.M.. “Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 Å Resolution”. Science. 1994. 266(5182): 75–81.
138.
HeY.-X.ZhangN.-N.LiW.-F.JiaN., et al. “N-Terminal Domain of Bombyx Mori Fibroin Mediates the Assembly of Silk in Response to pH Decrease”. J. Mol. Biol. 2012. 418(3): 197–207.
139.
XiaoY.MaB.McElhenyD.ParthasarathyS., et al. “Aβ(1–42) Fibril Structure Illuminates Self-Recognition and Replication of Amyloid in Alzheimer's Disease”. Nat. Struct. Mol. Biol. 2015. 22(6): 499–505.
TammL.K.TatulianS.A.. “Infrared Spectroscopy of Proteins and Peptides in Lipid Bilayers”. Q. Rev. Biophys. 1997. 30(4): 365–429.
142.
RothschildK.J.. “The Early Development and Application of FT-IR Difference Spectroscopy to Membrane Proteins: A Personal Perspective”. Biomed. Spectrosc. Imaging. 2016. 5(3): 231–267.
143.
BrownM.F.. “UV–Visible and Infrared Methods for Investigating Lipid–Rhodopsin Membrane Interactions”. In: VaidehiN.Klein-SeetharamanJ., editors. Membrane Protein Structure and Dynamics: Methods and Protocols. Totowa, NJ: Humana Press, 2012. Chapter I.8, Pp. 127–153.
144.
BaenzigerJ.E.RyanS.E.Kane-DicksonV.C.. “Membrane Receptor–Ligand Interactions Probed by Attenuated Total Reflectance Infrared Difference Spectroscopy”. In: GregoriouVasilis G.BraimanM.S., editors. Vibrational Spectroscopy of Biological and Polymeric Materials. Baton Rouge: Taylor and Francis Group, 2005. Chapter 7, Pp. 325–352.
145.
KomatsuH.LiuL.MurrayI.V.AxelsenP.H.. “A Mechanistic Link Between Oxidative Stress and Membrane Mediated Amyloidogenesis Revealed by Infrared Spectroscopy”. Biochim. Biophys. Acta. 2007. 1768(8): 1913–1922.
146.
DelangeF.Bovee-GeurtsP.H.M.PistoriusA.M.A.RothschildK.J.DegripW.J.. “Probing Intramolecular Orientations in Rhodopsin and Metarhodopsin II by Polarized Infrared Difference Spectroscopy”. Biochemistry. 1999. 38(40): 13200–13209.
147.
KandoriH.KinoshitaN.ShichidaY.MaedaA.. “Protein Structural Changes in Bacteriorhodopsin Upon Photoisomerization as Revealed by Polarized FT-IR Spectroscopy”. J. Phys. Chem. B. 1998. 102(40): 7899–7905.
148.
NabedrykE.GaravitoR.M.BretonJ.. “The Orientation of Beta-Sheets in Porin. A Polarized Fourier Transform Infrared Spectroscopic Investigation”. Biophys. J. 1988. 53(5): 671–676.
149.
BuchetR.VargaS.SeidlerN.W.MolnarE.MartonosiA.. “Polarized Infrared Attenuated Total Reflectance Spectroscopy of the Ca2+-ATpase of Sacroplasmic Reticulum”. Biochim. Biophys. Acta. 1991. 1068(2): 201–216.
150.
RaussensV.De JonghH.PezoletH.RuysschaertJ.M.GoormaghtighE.. “Secondary Structure of the Intact H+,K+-ATpase and of Its Membrane-Embedded Region: An Attenuated Total Reflection Infrared Spectroscopy, Circular Dichroism and Raman Spectroscopy Study”. Eur. J. Biochem. 1998. 252(2): 261–267.
151.
RaussensV.Le MaireM.RuysschaertJ.M.GoormaghtighE.. “Secondary Structure of the Membrane-Bound Domains of H+,K+-ATpase and Ca2+-Atpase, a Comparison by FTIR After Proteolysis Treatment of the Native Membranes”. FEBS Lett. 1998. 437(3): 187–192.
152.
BeeversA.J.KukolA.. “Secondary Structure, Orientation, Oligomerization of Phospholemman, a Cardiac Transmembrane Protein”. Protein Sci. 2006. 15(5): 1127–1132.
153.
Le CoutreJ.KabackH.R.PatelC.K.N.HeginbothamL.MillerC.. “Fourier Transform Infrared Spectroscopy Reveals a Rigid Alpha-Helical Assembly for the Tetrameric Streptomyces Lividans K+ Channel”. Proc. Natl. Acad. Sci. U.S.A. 1998. 95(11): 6114–6117.
154.
SabaR.I.RuysschaertJ.M.HerchuelzA.GoormaghtighE.. “Fourier Transform Infrared Spectroscopy Study of the Secondary and Tertiary Structure of the Reconstituted Na+/Ca2+ Exchanger 70 kDa Polypeptide”. J. Biol. Chem. 1999. 274(22): 15510–15518.
155.
KukolA.ArkinI.T.. “Structure of the Influenza C Virus CM2 Protein Transmembrane Domain Obtained by Site-Specific Infrared Dichroism and Global Molecular Dynamics Searching”. J. Biol. Chem. 2000. 275(6): 4225–4229.
156.
GanS.W.NgL.F.LinX.GongX.D.TorresJ.. “Structure and Ion Channel Activity of the Human Respiratory Syncytial Virus (hRSV) Small Hydrophobic Protein Transmembrane Domain”. Protein Sci. 2008. 17(5): 813–820.
157.
FahmyK.SakmarT.P.. “Interdisciplinary Biophysical Studies of Membrane Proteins Bacteriorhodopsin and Rhodopsin”. Biophys. Rev. 2022. 15(1): 111–125.
158.
GrimardV.ViganoC.MargollesA.WattiezR., et al. “Structure and Dynamics of the Membrane-Embedded Domain of Lmra Investigated by Coupling Polarized ATR FT-IR Spectroscopy and H-1/H-2 Exchange”. Biochemistry. 2001. 40(39): 11876–11886.
159.
AnbazhaganV.VijayN.KleinschmidtJ.H.MarshD.. “Protein-Lipid Interactions with Fusobacterium Nucleatum Major Outer Membrane Protein Foma: Spin-Label EPR and Polarized Infrared Spectroscopy”. Biochemistry. 2008. 47(32): 8414–8423.
160.
AgopianA.QuetinM.CastanoS.. “Structure and Interaction with Lipid Membrane Models of Semliki Forest Virus Fusion Peptide”. Biochim. Biophys. Acta. 2016. 1858(11): 2671–2680.
161.
RamakrishnanM.QuJ.PocanschiC.L.KleinschmidtJ.H.MarshD.. “Orientation of Beta-Barrel Proteins oMPA and fHUA in Lipid Membranes. Chain Length Dependence from Infrared Dichroism”. Biochemistry. 2005. 44(9): 3515–3523.
162.
HolmesD.F.LuY.H.StarborgT.KadlerK.E.. “Collagen Fibril Assembly and Function”. In: LitscherE.S.WassarmanP.M., editors. Extracellular Matrix and Egg Coats. Cambridge, MA: Elsevier Inc., 2018. Chapter 3, Pp. 107–142.
163.
SpalazziJ.P.BoskeyA.L.PleshkoN.LuH.H.. “Quantitative Mapping of Matrix Content and Distribution Across the Ligament-to-Bone Insertion”. PLoS One. 2013. 8(9): E74349.
164.
KhanarianN.T.BoushellM.K.SpalazziJ.P.PleshkoN., et al. “FT-IR-I Compositional Mapping of the Cartilage-to-Bone Interface as a Function of Tissue Region and Age”. J. Bone Miner. Res. 2014. 29(12): 2643–2652.
165.
ItoT.KanazawaK.Kimura-SudaH.. “Analysis of Collagen Fiber Orientation in Bone of Different Aged Rats Using FT-IR Imaging”. Mol. Cryst. Liq. Cryst. 2015. 622(1): 114–119.
166.
Kimura-SudaH.ItoT.KanazawaK.ChakiN.AkiyamaH.. “Collagen Fiber Orientation in the Femur of Rats with Chronic Kidney Disease”. E-J. Surf. Sci. Nanotechnol. 2015. 13: 244–246.
167.
ItoT.Kimura-SudaH.. “Analysis of Collagen Fiber Orientation in Bone Using Infrared Dichroism Imaging in Reflectance Mode”. Mol. Cryst. Liq. Cryst. 2017. 654(1): 244–248.
168.
ItoT.Kimura-SudaH.. “Degree of Orientations of Collagen Fibers and Bone Apatite Crystals in Rat Femora by Infrared Dichroism Imaging”. J. Oral Biosci. 2019. 61(2): 115–119.
169.
VrahnasC.BlankM.DiteT.A.TatarczuchL., et al. “Increased Autophagy in Ephrinb2-Deficient Osteocytes is Associated with Elevated Secondary Mineralization and Brittle Bone”. Nat. Commun. 2019. 10(1): 3436.
170.
VrahnasC.PearsonT.A.BruntA.R.ForwoodM.R., et al. “Anabolic Action of Parathyroid Hormone (PTH) Does Not Compromise Bone Matrix Mineral Composition or Maturation”. Bone. 2016. 93: 146–154.
171.
WestP.A.TorzilliP.A.ChenC.LinP.CamachoN.P.. “Fourier Transform Infrared Imaging Spectroscopy Analysis of Collagenase-Induced Cartilage Degradation”. J. Biomed. Opt. 2005. 10(1): 014015.
172.
YinJ.H.XiaY.. “Chemical Visualization of Individual Chondrocytes in Articular Cartilage by Attenuated-Total-Reflection Fourier Transform Infrared Microimaging”. Biomed. Opt. Express. 2011. 2(4): 937–945.
173.
LeeJ.H.XiaY.. “Quantitative Zonal Differentiation of Articular Cartilage by Microscopic Magnetic Resonance Imaging, Polarized Light Microscopy, Fourier-Transform Infrared Imaging”. Microsc. Res. Tech. 2013. 76(6): 625–632.
174.
Eklouh-MolinierC.NguyenT.T.SebiskveradzeD.FeruJ., et al. “Interest of Polarized FT-IR Imaging to Characterize the Collagen Network in Human Skin”. Biomed. Spectrosc. Imaging. 2014. 3(3): 281–286.
175.
NguyenT.T.Eklouh-MolinierC.SebiskveradzeD.FeruJ., et al. “Changes of Skin Collagen Orientation Associated with Chronological Aging as Probed by Polarized-FT-IR Micro-Imaging”. Analyst. 2014. 139(10): 2482–2488.
176.
VincentelliR.. “Relation Between Collagen Fiber Orientation and Age of Osteon Formation in Human Tibial Compact Bone”. Acta Anat. 1978. 100(1): 120–128.
177.
WarshawJ.BromageT.G.TerranovaC.J.EnlowD.H.. “Collagen Fiber Orientation in Primate Long Bones”. Anat. Rec. 2017. 300(7): 1189–1207.
178.
BakbakS.KayacanR.AkkuşO.. “Effect of Collagen Fiber Orientation on Mechanical Properties of Cortical Bone”. J. Biomech. 2011. 44(Suppl 1): 11.
179.
OzasaR.IshimotoT.MiyabeS.HashimotoJ., et al. “Osteoporosis Changes Collagen/Apatite Orientation and Young’s Modulus in Vertebral Cortical Bone of Rat”. Calcif. Tissue Int. 2019. 104(4): 449–460.
180.
GauciS.J.StantonH.LittleC.B.FosangA.J.. “Proteoglycan and Collagen Degradation in Osteoarthritis”. In: GrässelS.AszódiA., editors. Cartilage: Volume 2: Pathophysiology. Cham: Springer International Publishing, 2017. Chapter 3, Pp. 41–61.
181.
StylianouA.. “Assessing Collagen D-Band Periodicity with Atomic Force Microscopy”. Materials. 2022. 15(4): 1608.
182.
HondaR.RyuM.MoritakeM.BalčytisA., et al. “Infrared Polariscopy Imaging of Linear Polymeric Patterns with a Focal Plane Array”. Nanomaterials. 2019. 9(5): 1–13.
183.
IshimotoT.NakanoT.UmakoshiY.YamamotoM.TabataY.. “Degree of Biological Apatite C-Axis Orientation Rather Than Bone Mineral Density Controls Mechanical Function in Bone Regenerated Using Recombinant Bone Morphogenetic Protein-2”. J. Bone Miner. Res. 2013. 28(5): 1170–1179.
184.
ClarkS.M.IballJ.. “Orientation of Apatite Crystals in Bone”. Nature. 1954. 174(4426): 399–400.
SutherlandG.B.B.M.TsuboiM.. “The Infra-Red Spectrum and Molecular Configuration of Sodium Deoxyribonucleate”. Proc. R. Soc. London, Ser. A. 1957. 239(1219): 446–463.
187.
WoodB.R.. “The Importance of Hydration and DNA Conformation in Interpreting Infrared Spectra of Cells and Tissues”. Chem. Soc. Rev. 2016. 45(7): 1980–1998.
188.
MarvinD.A.SpencerM.WilkinsM.H.F.HamiltonL.D.. “A New Configuration of Deoxyribonucleic Acid”. Nature. 1958. 182(4632): 387–388.
189.
MitsuiY.LangridgeR.ShortleB.E.CantorC.R., et al. “Physical and Enzymatic Studies on Poly D(I–C).Poly D(I–C), an Unusual Double-Helical DNA”. Nature. 1970. 228(5277): 1166–1169.
190.
PohlF.M.JovinT.M.. “Salt-Induced Co-Operative Conformational Change of a Synthetic DNA: Equilibrium and Kinetic Studies with Poly(dG-dC)”. J. Mol. Biol. 1972. 67(3): 375–396.
191.
HeinemannU.RoskeY.. “Symmetry in Nucleic-Acid Double Helices”. Symmetry. 2020. 12(5): 737.
192.
FlemmingJ.PohleW.WellerK.. “Base Inclination of A- and B-DNA in Oriented Films as Revealed by Infrared Linear Dichroism”. Int. J. Biol. Macromol. 1988. 10(4): 248–254.
193.
PiletJ.BrahmsJ.. “Investigation of DNA Structural Changes by Infrared Spectroscopy”. Biopolymers. 1973. 12(2): 387–403.
194.
ChampellP.BrahmsJ.. “Conformational Properties of Some Viral DNAs”. Eur. J. Biochem. 1974. 45(1): 253–259.
195.
FritzscheH.PohleW.LangH.. “Conformational Study of Ultraviolet-Irradiated DNA by Infrared Dichroism”. Stud. Biophys. 1976. 55(2): 113–116.
196.
PiletJ.LengM.. “Comparison of Poly(dG-dC).Poly(dG-dC) Conformations in Oriented Films and in Solution”. Proc. Natl. Acad. Sci. U.S.A. 1982. 79(1): 26–30.
197.
BrahmsJ.PiletJ.Phuong LanT.T.HillL.R.. “Direct Evidence of the C-Like Form of Sodium Deoxyribonucleate”. Proc. Natl. Acad. Sci. U.S.A. 1973. 70(12): 3352–3355.
198.
BeetzC.P.AscarelliG.ArnottS.. “A Reinterpretation of the Infrared Linear Dichroism of Oriented Nucleic Acid Films and a Calculation of Some Effective Partial Changes on the Ribose Phosphate Backbone”. Biophys. J. 1979. 28(1): 15–26.
199.
LuK.C.Van ZandtL.L.ProhofskyE.W.. “Displacements of Backbone Vibrational Modes of A-DNA and B-DNA”. Biophys. J. 1979. 28(1): 27–32.
200.
PremilatS.AlbiserG.. “Conformations of A-DNA and B-DNA in Agreement With Fiber X-ray and Infrared Dichroism”. Nucleic Acids Res. 1983. 11(6): 1897–1908.
201.
PremilatS.AlbiserG.. “Conformations of C-DNA in Agreement With Fiber X-ray and Infrared Dichroism”. J. Biomol. Struct. Dyn. 1984. 2(3): 607–613.
202.
ZhengG.H.LuX.J.OlsonW.K.. “Web 3DNA-A Web Server for the Analysis, Reconstruction, and Visualization of Three-Dimensional Nucleic-Acid Structures”. Nucleic Acids Res. 2009. 37(Suppl. 2): W240–W246.
203.
PatroL.P.P.KumarA.KolimiN.RathinavelanT.. “3D-NuS: A Web Server for Automated Modeling and Visualization of Non-Canonical 3-Dimensional Nucleic Acid Structures”. J. Mol. Biol. 2017. 429(16): 2438–2448.
204.
PohleW.ZhurkinV.B.FritzscheH.. “The DNA Phosphate Orientation. Infrared Data and Energetically Favorable Structures”. Biopolymers. 1984. 23(11): 2603–2622.
205.
FritzscheH.RupprechtA.RichterM.. “Infrared Linear Dichroism of Oriented DNA-Ligand Complexes Prepared with the Wet-Spinning Method”. Nucleic Acids Res. 1984. 12(23): 9165–9177.
206.
FritzscheH.. “Infrared Linear Dichroism as a Tool to Monitor Antitumor Drug-Induced Changes of the Conformational Flexibility of Biopolymers”. J. Mol. Struct. 1990. 219: 275–280.
207.
FritzscheH.RupprechtA.. “Nucleic Acids–Drug-Interactions Studied by Infrared Linear Dichroism”. Paper presented at: 4th European Conference on the Spectroscopy of Biological Molecules. York, England;Sept 1–6 1991. Vol. 94, Pp. 379–380.
208.
FritzscheH.. “Infrared Linear Dichroism Studies of DNA-Drug Complexes: Quantitative Determination of the Drug-Induced Restriction of the B-A Transition”. Nucleic Acids Res. 1994. 22(5): 787–791.
209.
FritzscheH.ZimmerC.BurckhardtG.FortschI., et al. “Ligand-Induced Conformational Transition of DNA as Studied by Infrared Spectroscopy, Infrared Linear Dichroism, Circular Dichroism, Fluorescence Spectroscopy”. Paper presented at: 6th European Conference on Spectroscopy of Biological Molecules. Villeneuve d’Ascq, France;Sept 3–8 1995. Vol. 6, Pp. 339–340.
210.
TsuboiM.KuboY.IkedaT.OvermanS.A., et al. “Protein and DNA Residue Orientations in the Filamentous Virus Pf1 Determined by Polarized Raman and Polarized FT-IR Spectroscopy”. Biochemistry. 2003. 42(4): 940–950.
211.
Le SauxA.RuysschaertJ.-M.GoormaghtighE.. “Membrane Molecule Reorientation in an Electric Field Recorded by Attenuated Total Reflection Fourier-Transform Infrared Spectroscopy”. Biophys. J. 2001. 80(1): 324–330.
212.
ScheibeC.HauserK.. “Orientation of Lipids in Solid Supported Lipid Bilayers Studied by Polarized ATR FT-IR Spectroscopy”. Biomed. Spectrosc. Imaging. 2018. 7(1–2): 17–24.
213.
CitraM.J.AxelsenP.H.. “Determination of Molecular Order in Supported Lipid Membranes by Internal Reflection Fourier Transform Infrared Spectroscopy”. Biophys. J. 1996. 71(4): 1796–1805.
214.
HarrickN.J.BeckmannK.H.. “Internal Reflection Spectroscopy”. In: KaneP.F.LarrabeeG.B., editors. Characterization of Solid Surfaces. Boston, MA: Springer, 1974. Chapter 10, Pp. 215–245.
215.
FringeliU.P.. “In Situ Infrared Attenuated Total Reflection (IR ATR) Spectroscopy: A Complementary Analytical Tool for Drug Design and Drug Delivery”. Chimia. 1992. 46(5): 200.
216.
PicardF.BuffeteauT.DesbatB.AugerM.PézoletM.. “Quantitative Orientation Measurements in Thin Lipid Films by Attenuated Total Reflection Infrared Spectroscopy”. Biophys. J. 1999. 76(1): 539–551.
217.
PetrusJ.Czarnik-MatusewiczB.. “Investigation of the Polarization Dependent Attenuated Total Reflection Infrared Spectra of Ordered Lipids Assisted by Principal Component Analysis”. Vib. Spectrosc. 2012. 62: 133–142.
218.
MorikawaH.HayashiR.SendaM.. “Infrared Analysis of Pea Stem Cell Walls and Oriented Structure of Matrix Polysaccharides in Them”. Plant Cell Physiol. 1978. 19(7): 1151–1159.
219.
MorikawaH.SendaM.. “Infrared Analysis of Oat Coleoptile Cell Walls and Oriented Structure of Matrix Polysaccharides in the Walls”. Plant Cell Physiol. 1978. 19(2): 327–336.
220.
HayashiR.MorikawaH.NakajimaN.IchikawaY.SendaM.. “Oriented Structure of Pectic Polysaccharides in Pea Epidermal Cell Walls”. Plant Cell Physiol. 1980. 21(6): 999–1005.
221.
McCannM.C.HammouriM.WilsonR.BeltonP.RobertsK.. “Fourier Transform Infrared Microspectroscopy is a New Way to Look at Plant Cell Walls”. Plant Physiol. 1992. 100(4): 1940–1947.
222.
McCannM.C.StaceyN.J.WilsonR.RobertsK.. “Orientation of Macromolecules in the Walls of Elongating Carrot Cells”. J. Cell Sci. 1993. 106(4): 1347–1356.
223.
ChenL.WilsonR.H.McCannM.C.. “Infra-Red Microspectroscopy of Hydrated Biological Systems: Design and Construction of a New Cell with Atmospheric Control for the Study of Plant Cell Walls”. J. Microsc. (Oxford, U.K.). 1997. 188(1): 62–71.
224.
McCannM.C.ChenL.RobertsK.KemsleyE.K., et al. “Infrared Microspectroscopy: Sampling Heterogeneity in Plant Cell Wall Composition and Architecture”. Physiol. Plant. 1997. 100(3): 729–738.
225.
Pruszyńska-KarbownikE.GutowskiP.KarbownikP.. “Optical Polarization Shift in Beams Emitted by Quantum Cascade Lasers”. Opt. Quantum Electron. 2019. 51(10): 325.
226.
KansizM.PraterC.DillonE.LoM., et al. “Optical Photothermal Infrared Microspectroscopy with Simultaneous Raman: A New Non-Contact Failure Analysis Technique for Identification of <10mm Organic Contamination in the Hard Drive and Other Electronics Industries”. Microsc. Today. 2020. 28(3): 26–36.
