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Volumn 107, Issue 6, 2012, Pages 205-212

Near infrared and two-dimensional correlation infrared spectroscopic study on the heat denaturation of collagen in aqueous solution

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE I; COLLAGEN MOLECULES; COLLAGEN TRIPLE HELIX; COMBINATION BANDS; DENATURED STATE; FREE WATER; HEAT DENATURATION; IMINO GROUPS; IN-SITU; INFRARED SPECTROSCOPIC STUDIES; NEAR INFRARED; NH GROUPS; SPECTRAL DATA; STATES OF WATER; TEMPERATURE EVOLUTION; THERMAL BEHAVIORS; THERMAL DENATURATION TRANSITIONS; TWO-DIMENSIONAL CORRELATION; TWO-DIMENSIONAL CORRELATION INFRARED SPECTROSCOPY; WATER MOLECULE;

EID: 84863713355     PISSN: 00029726     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (4)

References (43)
  • 3
    • 0032482162 scopus 로고    scopus 로고
    • Protein release from collagen matrices
    • DOI 10.1016/S0169-409X(97)00119-1, PII S0169409X97001191
    • Fujioka, K., Medal M., Hojo, T., and Sano A.; Protein Release from Collagen Matrices. Adv. Drug Delivery Rev. 31, 247-266, 1998. (Pubitemid 28191868)
    • (1998) Advanced Drug Delivery Reviews , vol.31 , Issue.3 , pp. 247-266
    • Fujioka, K.1    Maeda, M.2    Hojo, T.3    Sano, A.4
  • 4
    • 0036039198 scopus 로고    scopus 로고
    • Dynamic thermomechanical studies on collagen denaturation: A comparative study of bovine Pericardium and Chordae Tendinae
    • Jahangir, A., and Lee, J. M.; Dynamic Thermomechanical Studies on Collagen Denaturation: a Comparative Study of Bovine Pericardium and Chordae Tendinae. Biomed Scilnstrum. 38, 151-156, 2002. (Pubitemid 35005959)
    • (2002) Biomedical Sciences Instrumentation , vol.38 , pp. 151-156
    • Jahangir, A.1    Lee, J.M.2
  • 5
    • 77952358318 scopus 로고    scopus 로고
    • Cleavage site specificity selection in type i collagen degradation
    • Salsas-Escat, R., Nerenberg, P. S., and Stultz, C. M.; Cleavage Site Specificity Selection in Type I Collagen Degradation. Biochemistry 49, 4147-4158, 2010.
    • (2010) Biochemistry , vol.49 , pp. 4147-4158
    • Salsas-Escat, R.1    Nerenberg, P.S.2    Stultz, C.M.3
  • 6
    • 0018795178 scopus 로고
    • Thermal stability of the triple helix of type i procollagen and collagen. Precautions for minimizing ultraviolet damage to proteins during circular dichroism studies
    • Hayashi, T., Curran-Patel, S., and Prockop, D. J.; Thermal Stability of the Triple Helix of Type I Procollagen and Collagen. Precautions for Minimizing Ultraviolet Damage to Proteins during Circular Dichroism Studies. Biochemistry 18, 4182-4187, 1979.
    • (1979) Biochemistry , vol.18 , pp. 4182-4187
    • Hayashi, T.1    Curran-Patel, S.2    Prockop, D.J.3
  • 7
    • 0030107381 scopus 로고    scopus 로고
    • Structural effects of cross-linking reagents on triple-helix reformation of intramolecularly cross-linked collagen
    • DOI 10.1016/0032-3861(96)80856-1
    • Watanabe, K., Nakagawa, J., Ebihara, T., and Okamoto, Y; Structral Effects of Cross-linking Reagents on Triplehelix Reformation of Intramolecularly Cross-linked Collagen. Polymer 37, 1285-1288, 1996. (Pubitemid 126397008)
    • (1996) Polymer , vol.37 , Issue.7 , pp. 1285-1288
    • Watanabe, K.1    Nakagawa, J.2    Ebihara, T.3    Okamoto, Y.4
  • 8
    • 0031341473 scopus 로고    scopus 로고
    • Configuration between Re-formed collagen triple helices and artificially introduced cross-links in gelatin gels
    • Watanabe, K., Tezuka, Y. and Ishii, T.; Configuration Between Re-formed Collagen Triple Helices and Artificially Introduced Cross-links in Gelatin Gel. Macromolecules 30, 7910-7913, 1997. (Pubitemid 127561618)
    • (1997) Macromolecules , vol.30 , Issue.25 , pp. 7910-7913
    • Watanabe, K.1    Tezuka, Y.2    Ishii, T.3
  • 9
    • 0345688751 scopus 로고    scopus 로고
    • Characterization of gelatin and acid soluble collagen by size exclusion chromatography coupled with multi angle light scattering(SEC-MALS)
    • Meyer, M., and Morgenstern, B.; Characterization of Gelatin and Acid Soluble Collagen by Size Exclusion Chromatography Coupled with Multi Angle Light Scattering(SEC-MALS). Biomacromolecules 4, 1727-1732, 2003.
    • (2003) Biomacromolecules , vol.4 , pp. 1727-1732
    • Meyer, M.1    Morgenstern, B.2
  • 10
    • 0014737293 scopus 로고
    • Thermal conformational transformation of topocollagen. I. Calorimetric study
    • Privalov, P. L., and Tiktopulo, E. I.; Thermal Conformational Transformation of Topocollagen. I. Calorimetric Study. Biopolymers 9, 127-139, 1970.
    • (1970) Biopolymers , vol.9 , pp. 127-139
    • Privalov, P.L.1    Tiktopulo, E.I.2
  • 12
    • 0028918983 scopus 로고
    • The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry
    • Miles, C. A., Burjanadze, T. V., and Bailey, A. J.; The Kinetics of the Thermal Denaturation of Collagen in Unrestrained Rat Tail Tendon Determined by Differential Scanning Calorimetry. J Mol. Biol. 245, 437-446, 1995.
    • (1995) J Mol. Biol. , vol.245 , pp. 437-446
    • Miles, C.A.1    Burjanadze, T.V.2    Bailey, A.J.3
  • 13
    • 0032549578 scopus 로고    scopus 로고
    • Differences between the thermal stabilities of the three triple-helical domains of type IX collagen
    • DOI 10.1006/jmbi.1997.1603
    • Miles, C. A., Knott, L., Sumner, I. G., and Bailey, A. J.; Difference Between the Thermal Stabilities of the Three Triple-helical Domains of Type IX Collagen. J Mol. Biol. 277, 135-144, 1998. (Pubitemid 28151887)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.1 , pp. 135-144
    • Miles, C.A.1    Knott, L.2    Sumner, I.G.3    Bailey, A.J.4
  • 14
    • 12544255038 scopus 로고    scopus 로고
    • The increase in denaturation temperature following cross-linking of collagen is caused by dehydration of the fibers
    • Miles, C. A., Avery, N. C., Rodin, V. V., and Bailey, A. J.; The Increase in Denaturation Temperature Following Cross-linking of Collagen is Caused by Dehydration of the Fibers. J Mol. Biol. 346, 551-556, 2005.
    • (2005) J Mol. Biol. , vol.346 , pp. 551-556
    • Miles, C.A.1    Avery, N.C.2    Rodin, V.V.3    Bailey, A.J.4
  • 17
    • 71649087577 scopus 로고    scopus 로고
    • 13C NMR studies on the temperature-dependent water and protein dynamics in hydrated elastin, myoglobin and collagen
    • 13C NMR Studies on the Temperature-dependent Water and Protein Dynamics in Hydrated Elastin, Myoglobin and Collagen. BBA Proteins and Proteomics 1804, 41-48, 2010.
    • (2010) BBA Proteins and Proteomics , vol.1804 , pp. 41-48
    • Lusceaca, S.A.1    Vogela, M.R.2    Herbersb, C.R.3
  • 18
    • 36649007437 scopus 로고    scopus 로고
    • Ultrastructural studies on the collagen of the marine sponge Chondrosia reniformis nardo
    • DOI 10.1021/bm700574y
    • Heinemann, S., Ehrlich, H., Douglas, T., Heinemann, C., Worch, H., Schatton, W., and Hanke, T.; Ultrastructural Studies on the Collagen of the Marine Sponge Chondrosia Reniformis Nardo. Biomacromolecules 8, 3452-3457, 2007. (Pubitemid 350193745)
    • (2007) Biomacromolecules , vol.8 , Issue.11 , pp. 3452-3457
    • Heinemann, S.1    Ehrlich, H.2    Douglas, T.3    Heinemann, C.4    Worch, H.5    Schatton, W.6    Hanke, T.7
  • 19
    • 34250689930 scopus 로고    scopus 로고
    • Study of electron transfer in ferrocene-labeled collagen-like peptides
    • DOI 10.1021/la070175n
    • Dey, S. K., Long, Y. T., Chowdhury, S., Sutherland, T. C., Mandai, H. S., and Kraatz, H. B.; Study of Electron Transfer in Ferrocene-labeled Collagen-like Peptides. Langmuir 23, 6475-6477, 2007. (Pubitemid 46943465)
    • (2007) Langmuir , vol.23 , Issue.12 , pp. 6475-6477
    • Dey, S.K.1    Long, Y.-T.2    Chowdhury, S.3    Sutherland, T.C.4    Mandal, H.S.5    Kraatz, H.-B.6
  • 20
    • 59849108384 scopus 로고    scopus 로고
    • Structural transition during thermal denaturation of collagen in the solution and film states
    • Shanmugam, G., and Polavarapu, P. L.; Structural Transition during Thermal Denaturation of Collagen in the Solution and Film States. Chirality 21, 152-159, 2009.
    • (2009) Chirality , vol.21 , pp. 152-159
    • Shanmugam, G.1    Polavarapu, P.L.2
  • 22
    • 33746239552 scopus 로고    scopus 로고
    • Molecular dynamics study onset of water gelation around the collagen triple helic
    • Handgraaf, J. W., and Zerbetto, F.; Molecular Dynamics Study Onset of Water Gelation Around the Collagen Triple Helic. Proteins: Structure Function and Genetics 64,711-718, 2006.
    • (2006) Proteins: Structure Function and Genetics , vol.64 , pp. 711-718
    • Handgraaf, J.W.1    Zerbetto, F.2
  • 23
    • 34250748568 scopus 로고    scopus 로고
    • Effect of the structural water on the mechanical properties of collagen-like microfibrils: A molecular dynamics study
    • DOI 10.1007/s10439-007-9296-8
    • Zhang, D., Chippada, U., and Jordan, K.; Effect of Structural Water on the Mechanical Properties of Collagen like Microfibrils: a Molecular Dynamics Study. Ann. Biomed. Eng. 35, 1216-1230, 2007. (Pubitemid 46966271)
    • (2007) Annals of Biomedical Engineering , vol.35 , Issue.7 , pp. 1216-1230
    • Zhang, D.1    Chippada, U.2    Jordan, K.3
  • 25
    • 0030560866 scopus 로고    scopus 로고
    • Basic thermoanalytical studies of insoluble collagen matrices
    • Friess, W., and Lee, G.; Basic Thermoanalytical Studies of Insoluble Collagen Matrices. Biomaterials 17, 2289-2294, 1996.
    • (1996) Biomaterials , vol.17 , pp. 2289-2294
    • Friess, W.1    Lee, G.2
  • 27
    • 0014975333 scopus 로고
    • Deuterium NMR and EPR of hydrated collagen fibers in the presence of salts
    • Fung, B. M., and Trautmann, R; Deuterium NMR and EPR of Hydrated Collagen Fibers in the Presence of Salts. Biopolymers 10, 391-397, 1971.
    • (1971) Biopolymers , vol.10 , pp. 391-397
    • Fung, B.M.1    Trautmann, R.2
  • 28
    • 0015531034 scopus 로고
    • The ordering and reaxation times of water adsorbed on collagen fibers
    • Fung, B. M., and Siegel, M. M.; The Ordering and Reaxation Times of Water Adsorbed on Collagen Fibers. Biochem.Biophys. Acta 278, 185-187, 1972.
    • (1972) Biochem.Biophys. Acta , vol.278 , pp. 185-187
    • Fung, B.M.1    Siegel, M.M.2
  • 29
    • 0015799943 scopus 로고
    • The effect of alkali and alkine earth salts on the structure of hydrated collagen fibers as studied by deuterium NMR
    • Fung, B. M., and Wei, S. C.; The Effect of Alkali and Alkine Earth Salts on the Structure of Hydrated Collagen Fibers as Studied by Deuterium NMR. Biopolymers 12, 1053-1062, 1973.
    • (1973) Biopolymers , vol.12 , pp. 1053-1062
    • Fung, B.M.1    Wei, S.C.2
  • 30
    • 0016264117 scopus 로고
    • The structure of water absorbed in collagen. I. The dielectric properties
    • Hoeve, C. A. J., and Lue, P. C.; The Structure of Water Absorbed in Collagen. I. the Dielectric Properties. Biopolymers 13, 1661-1680, 1974.
    • (1974) Biopolymers , vol.13 , pp. 1661-1680
    • Hoeve, C.A.J.1    Lue, P.C.2
  • 31
    • 0001004843 scopus 로고
    • The structure of water absorbed in collagen
    • Hoeve, C. A. J., and Tata, A. S.; The Structure of Water Absorbed in Collagen. J. Phys. Chem. 82, 1660-1663, 1978.
    • (1978) J. Phys. Chem. , vol.82 , pp. 1660-1663
    • Hoeve, C.A.J.1    Tata, A.S.2
  • 32
    • 0014737293 scopus 로고
    • Thermal conformational transformation of tropocollagen
    • Privalov, P. L., and Tiktopulo, E. L.; Thermal Conformational Transformation of Tropocollagen. Biopolymers 9, 127-139, 1970.
    • (1970) Biopolymers , vol.9 , pp. 127-139
    • Privalov, P.L.1    Tiktopulo, E.L.2
  • 34
    • 79960275171 scopus 로고    scopus 로고
    • The futher investigation of tanning mechanisms of typical tannages by ultraviolet- visible near infrared dffused reflectance spectrophotometry
    • Guo, J. L., Huang, X., Wu, C., Liao, X. P., and Shi, B.; The Futher Investigation of Tanning Mechanisms of Typical Tannages by Ultraviolet- visible near Infrared Dffused Reflectance Spectrophotometry. JALCA 106, 226-231, 2011.
    • (2011) JALCA , vol.106 , pp. 226-231
    • Guo, J.L.1    Huang, X.2    Wu, C.3    Liao, X.P.4    Shi, B.5
  • 35
    • 34547356798 scopus 로고    scopus 로고
    • Structure analysis of poly (N-isopropylacrylamide) using near-infrared spectroscopy and generalized two-dimensional correlation infrared spectroscopy
    • Sun, B. J., Lin, Y. A., and Wu, P. Y.; Structure Analysis of poly (N-isopropylacrylamide) Using Near-infrared Spectroscopy and Generalized Two-dimensional Correlation Infrared Spectroscopy. Appl. Spectrosc. 61, 765-771, 2007.
    • (2007) Appl. Spectrosc. , vol.61 , pp. 765-771
    • Sun, B.J.1    Lin, Y.A.2    Wu, P.Y.3
  • 36
    • 0000857228 scopus 로고    scopus 로고
    • Two-dimensional fourier transform near-infrared spectroscopy study of heat denaturation of ovalbumin in aqueous solutions
    • Wang, Y., Murayama, K., Myojo, Y., Tsenkova, R., Hayashi, N., and Ozaki, Y; Two-dimensional Fourier Transform Near-infrared Spectroscopy Study of Heat Denaturation of Ovalbumin in Aqueous Solution. J. Phys. Chem. 102, 6655-6662, 1998. (Pubitemid 128586698)
    • (1998) Journal of Physical Chemistry B , vol.102 , Issue.34 , pp. 6655-6662
    • Wang, Y.1    Murayama, K.2    Myojo, Y.3    Tsenkova, R.4    Hayashi, N.5    Ozaki, Y.6
  • 37
    • 0034226886 scopus 로고    scopus 로고
    • Determination of two-dimensional correlation spectra using the hubert transform
    • Noda, I.; Determination of Two-dimensional Correlation Spectra Using the Hubert Transform. Appl. Spectrosc. 54, 994-999,2000.
    • (2000) Appl. Spectrosc. , vol.54 , pp. 994-999
    • Noda, I.1
  • 38
    • 0001572782 scopus 로고
    • Near infrared spectroscopy and chemometrics studies of temperature-dependent spectral variation of water: Relationship between spectral changes and hydrogen bonds
    • Maeda, H., Ozaki, Y., Tanaka, M., Hayashi, N., and Kojima, T.; Near Infrared Spectroscopy and Chemometrics Studies of Temperature-dependent Spectral Variation of Water: Relationship between Spectral Changes and Hydrogen Bonds. J. Near Infrared Spectrosc. 3, 191-201, 1995.
    • (1995) J. Near Infrared Spectrosc. , vol.3 , pp. 191-201
    • Maeda, H.1    Ozaki, Y.2    Tanaka, M.3    Hayashi, N.4    Kojima, T.5
  • 39
    • 0142135858 scopus 로고    scopus 로고
    • Modeling temperature-dependent protein structure transition by combined Near-IR and Mid-IR spectroscopies and multivariate curve resolution
    • Navea, S., de Juan, A., and Tauler, R.; Modeling Temperature-dependent Protein Structure Transition by Combined Near-IR and Mid-IR Spectroscopies and Multivariate Curve Resolution. Anal. Chem. 75, 5592-5601, 2003.
    • (2003) Anal. Chem. , vol.75 , pp. 5592-5601
    • Navea, S.1    De Juan, A.2    Tauler, R.3
  • 40
    • 0016706937 scopus 로고
    • Infrared spectroscopy of collagen-like polypeptide
    • Doyle, B. B., Bendit, E. G., and Blout, E. R.; Infrared Spectroscopy of Collagen-like Polypeptide. Biopolymers 14, 937-957, 1975.
    • (1975) Biopolymers , vol.14 , pp. 937-957
    • Doyle, B.B.1    Bendit, E.G.2    Blout, E.R.3
  • 42
    • 34447570983 scopus 로고    scopus 로고
    • Temperature induced denaturation of collagen in acidic solution
    • DOI 10.1002/bip.20742
    • Mu, C., Li, D., Lin, W., Ding, Y., and Zhang, G.; Temperature Induced Denaturation of Collagen in Acidic Solution. Biopolymers 86, 282-287, 2007. (Pubitemid 47067545)
    • (2007) Biopolymers , vol.86 , Issue.4 , pp. 282-287
    • Mu, C.1    Li, D.2    Lin, W.3    Ding, Y.4    Zhang, G.5
  • 43
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella, J., Brodsky, B., and Bermanl, H. M.; Hydration Structure of a Collagen Peptide. Structure 3, 893-906, 1995.
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Bermanl, H.M.3


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