메뉴 건너뛰기




Volumn 548, Issue , 2012, Pages 1-5

Revisit the pre-transition of type i collagen denaturation in dilute solution by ultrasensitive differential scanning calorimetry

Author keywords

Amino acid sequence; Collagen; Denaturation; Pre transition; Triple helix

Indexed keywords

AMINO ACID SEQUENCE; DILUTE SOLUTION; PRE-TRANSITION; STRUCTURAL ORIGIN; STRUCTURAL TRANSITIONS; THERMAL DENATURATIONS; THERMOANALYTICAL STUDY; TRIPLE HELIXES; TYPE I COLLAGEN; ULTRASENSITIVE;

EID: 84865646292     PISSN: 00406031     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tca.2012.08.024     Document Type: Article
Times cited : (19)

References (39)
  • 2
    • 0025792023 scopus 로고
    • Collagen family of proteins
    • M. Van der Rest, and R. Garrone Collagen family of proteins FASEB J. 5 1991 2814 2822
    • (1991) FASEB J. , vol.5 , pp. 2814-2822
    • Van Der Rest, M.1    Garrone, R.2
  • 3
    • 25444463441 scopus 로고    scopus 로고
    • Structure, stability and folding of the collagen triple helix
    • DOI 10.1007/b103818, Collagen: Primer in Structure, Processing and Assembly
    • J. Engel, and H.P. Bächinger Structure, stability and folding of the collagen triple helix Top. Curr. Chem. 247 2005 7 33 (Pubitemid 44423496)
    • (2005) Topics in Current Chemistry , vol.247 , pp. 7-33
    • Engel, J.1    Bachinger, H.P.2
  • 4
    • 0028918983 scopus 로고
    • The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry
    • C.A. Miles, T.V. Burjanadze, and A.J. Bailey The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry J. Mol. Biol. 245 1995 437 446
    • (1995) J. Mol. Biol. , vol.245 , pp. 437-446
    • Miles, C.A.1    Burjanadze, T.V.2    Bailey, A.J.3
  • 5
    • 34447570983 scopus 로고    scopus 로고
    • Temperature induced denaturation of collagen in acidic solution
    • DOI 10.1002/bip.20742
    • C.D. Mu, D.F. Li, W. Lin, Y.W. Ding, and G.Z. Zhang Temperature induced denaturation of collagen in acidic solution Biopolymers 86 2007 282 287 (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
  • 7
    • 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
    • T. Hayashi, S. Curran-Patel, and D.J. Prockop 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 1979 4182 4187
    • (1979) Biochemistry , vol.18 , pp. 4182-4187
    • Hayashi, T.1    Curran-Patel, S.2    Prockop, D.J.3
  • 8
    • 0026910229 scopus 로고
    • Presence of a thermostable domain in the helical part of the type 1 collagen molecule and its role in the mechanism of triple helix folding
    • T.V. Burjanadze, and M.O. Bezhitadze Presence of a thermostable domain in the helical part of the type 1 collagen molecule and its role in the mechanism of triple helix folding Biopolymers 32 1992 951 956
    • (1992) Biopolymers , vol.32 , pp. 951-956
    • Burjanadze, T.V.1    Bezhitadze, M.O.2
  • 9
    • 0029837626 scopus 로고    scopus 로고
    • Acetyl-terminated and template-assembled collagen-based polypeptides composed of Gly-Pro-Hyp sequences. 2. Synthesis and conformational analysis by circular dichroism ultraviolet absorbance, and optical rotation
    • Y. Feng, G. Melacini, J.P. Taulane, and M. Goodman Acetyl-terminated and template-assembled collagen-based polypeptides composed of Gly-Pro-Hyp sequences. 2. Synthesis and conformational analysis by circular dichroism ultraviolet absorbance, and optical rotation J. Am. Chem. Soc. 118 1996 10351 10364
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10351-10364
    • Feng, Y.1    Melacini, G.2    Taulane, J.P.3    Goodman, M.4
  • 10
    • 0033930562 scopus 로고    scopus 로고
    • Influence of neutral salts on the hydrothermal stability of acid-soluble collagen
    • DOI 10.1023/A:1007074314686
    • E.M. Brown, H.M. Farrell, and R.J. Wildermuth Influence of neutral salts on the hydrothermal stability of acid-soluble collagen J. Protein Chem. 19 2000 85 92 (Pubitemid 30483392)
    • (2000) Journal of Protein Chemistry , vol.19 , Issue.2 , pp. 85-92
    • Brown, E.M.1    Farrell Jr., H.M.2    Wildermuth, R.J.3
  • 11
    • 78650041218 scopus 로고    scopus 로고
    • Effects of microwave irradiation on collagen denaturation
    • D.F. Li, C.D. Mu, Q. Zhang, Y.L. Zhou, and W. Lin Effects of microwave irradiation on collagen denaturation J. Food Biochem. 34 2010 1319 1331
    • (2010) J. Food Biochem. , vol.34 , pp. 1319-1331
    • Li, D.F.1    Mu, C.D.2    Zhang, Q.3    Zhou, Y.L.4    Lin, W.5
  • 12
    • 0023672083 scopus 로고
    • A study of the hydration and thermodynamics of warm-water and cold-water fish collagens
    • C. Rose, M. Kumar, and A.B. Mandal A study of the hydration and thermodynamics of warm-water and cold-water fish collagens Biochem. J. 249 1988 127 133
    • (1988) Biochem. J. , vol.249 , pp. 127-133
    • Rose, C.1    Kumar, M.2    Mandal, A.B.3
  • 13
    • 12544255038 scopus 로고    scopus 로고
    • The increase in denaturation temperature following cross-linking of collagen is caused by dehydration of the fibres
    • C.A. Miles, N.C. Avery, V.V. Rodin, and A.J. Bailey The increase in denaturation temperature following cross-linking of collagen is caused by dehydration of the fibres J. Mol. Biol. 346 2005 551 556
    • (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
  • 14
    • 0014737293 scopus 로고
    • Thermal conformational transformation of tropocollagen. I. calorimetric study
    • P.L. Privalov, and E.I. Tiktopulo Thermal conformational transformation of tropocollagen. I. calorimetric study Biopolymers 9 1970 127 139
    • (1970) Biopolymers , vol.9 , pp. 127-139
    • Privalov, P.L.1    Tiktopulo, E.I.2
  • 16
    • 0021146578 scopus 로고
    • Reconstituted collagen fibrils. Fibrillar and molecular stability of the collagen upon maturation in vitro
    • C.C. Danielsen Reconstituted collagen fibrils. Fibrillar and molecular stability of the collagen upon maturation in vitro Biochem. J. 222 1984 663 668 (Pubitemid 14007834)
    • (1984) Biochemical Journal , vol.222 , Issue.3 , pp. 663-668
    • Danielsen, C.C.1
  • 17
    • 0024083398 scopus 로고
    • Quantitation of collagen fragments and gelatin by deconvolution of polarimetry denaturation curves
    • R. Condell, N. Sakai, R. Mercado, and E. Larenas Quantitation of collagen fragments and gelatin by deconvolution of polarimetry denaturation curves Coll. Relat. Res. 8 1988 407 418
    • (1988) Coll. Relat. Res. , vol.8 , pp. 407-418
    • Condell, R.1    Sakai, N.2    Mercado, R.3    Larenas, E.4
  • 18
    • 0035385135 scopus 로고    scopus 로고
    • Hydrogels for tissue engineering
    • K.Y. Lee, and D.J. Mooney Hydrogels for tissue engineering Chem. Rev. 101 2001 1869 1880
    • (2001) Chem. Rev. , vol.101 , pp. 1869-1880
    • Lee, K.Y.1    Mooney, D.J.2
  • 21
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self-assembly and the development of tendon mechanical properties
    • DOI 10.1016/S0021-9290(03)00135-0
    • F.H. Silver, J.W. Freeman, and G.P. Seehra Collagen self-assembly and the development of tendon mechanical properties J. Biomech. 36 2003 1529 1553 (Pubitemid 37117360)
    • (2003) Journal of Biomechanics , vol.36 , Issue.10 , pp. 1529-1553
    • Silver, F.H.1    Freeman, J.W.2    Seehra, G.P.3
  • 22
    • 0018391677 scopus 로고
    • Hydroxyproline content and location in relation to collagen thermal stability
    • DOI 10.1002/bip.1979.360180413
    • T.V. Burjanadze Hydroxyproline content and location in relation to collagen thermal stability Biopolymers 18 1979 931 938 (Pubitemid 9188917)
    • (1979) Biopolymers , vol.18 , Issue.4 , pp. 931-938
    • Burjanadze, T.V.1
  • 23
    • 0035219275 scopus 로고    scopus 로고
    • Thermally labile domains in the collagen molecule
    • C. Miles, and A. Bailey Thermally labile domains in the collagen molecule Micron 32 2001 325 332
    • (2001) Micron , vol.32 , pp. 325-332
    • Miles, C.1    Bailey, A.2
  • 24
    • 47749145413 scopus 로고    scopus 로고
    • Triple-helical peptides: An approach to collagen conformation, stability, and self-association
    • B. Brodsky, G. Thiagarajan, B. Madhan, and K. Kar Triple-helical peptides: an approach to collagen conformation, stability, and self-association Biopolymers 89 2008 345 353
    • (2008) Biopolymers , vol.89 , pp. 345-353
    • Brodsky, B.1    Thiagarajan, G.2    Madhan, B.3    Kar, K.4
  • 25
    • 13444302895 scopus 로고    scopus 로고
    • Microcalorimetric investigation on aggregation and dissolution of poly (N-isopropylacrylamide) chains in water
    • Y.W. Ding, X.D. Ye, and G.Z. Zhang Microcalorimetric investigation on aggregation and dissolution of poly (N-isopropylacrylamide) chains in water Macromolecules 38 2005 904 908
    • (2005) Macromolecules , vol.38 , pp. 904-908
    • Ding, Y.W.1    Ye, X.D.2    Zhang, G.Z.3
  • 26
    • 34248190655 scopus 로고    scopus 로고
    • Collapse and aggregation of poly (N-isopropylacrylamide) chains in aqueous solutions crowded by polyethylene glycol
    • Y.W. Ding, and G.Z. Zhang Collapse and aggregation of poly (N-isopropylacrylamide) chains in aqueous solutions crowded by polyethylene glycol J. Phys. Chem. C 111 2007 5309 5312
    • (2007) J. Phys. Chem. C , vol.111 , pp. 5309-5312
    • Ding, Y.W.1    Zhang, G.Z.2
  • 27
    • 70349190396 scopus 로고    scopus 로고
    • Supramolecular assembly of electrostatically stabilized, hydroxyproline-lacking collagen mimetic peptides
    • O.D. Krishna, and K.L. Kiick Supramolecular assembly of electrostatically stabilized, hydroxyproline-lacking collagen mimetic peptides Biomacromolecules 10 2009 2626 2631
    • (2009) Biomacromolecules , vol.10 , pp. 2626-2631
    • Krishna, O.D.1    Kiick, K.L.2
  • 28
    • 0028417155 scopus 로고
    • Laser light-scattering characterization of gelatin in formamide
    • C. Wu Laser light-scattering characterization of gelatin in formamide J. Polym. Sci. Pol. Phys. 32 1994 803 810
    • (1994) J. Polym. Sci. Pol. Phys. , vol.32 , pp. 803-810
    • Wu, C.1
  • 29
    • 0037068139 scopus 로고    scopus 로고
    • Adsorption of gelatins on surfactant-free PS nanoparticles
    • T.J. Hu, J. Gao, H. Auweter, R. Iden, E. Lueddecke, and C. Wu Adsorption of gelatins on surfactant-free PS nanoparticles Polymer 43 2002 5545 5550
    • (2002) Polymer , vol.43 , pp. 5545-5550
    • Hu, T.J.1    Gao, J.2    Auweter, H.3    Iden, R.4    Lueddecke, E.5    Wu, C.6
  • 32
    • 33846637900 scopus 로고    scopus 로고
    • Microcalorimetry of biological macromolecules
    • DOI 10.1016/j.bpc.2006.05.004, PII S0301462206001608
    • P.L. Privalov, and A.I. Dragan Microcalorimetry of biological macromolecules Biophys. Chem. 126 2007 16 24 (Pubitemid 46186628)
    • (2007) Biophysical Chemistry , vol.126 , Issue.1-3 , pp. 16-24
    • Privalov, P.L.1    Dragan, A.I.2
  • 33
    • 0032987216 scopus 로고    scopus 로고
    • Stabilizing effect of glycerol on collagen type I isolated from different species
    • DOI 10.1016/S0308-8146(99)00097-7, PII S0308814699000977
    • R. Penkova, I. Goshev, S. Gorinstein, and P. Nedkov Stabilizing effect of glycerol on collagen type I isolated from different species Food Chem. 66 1999 483 487 (Pubitemid 29255862)
    • (1999) Food Chemistry , vol.66 , Issue.4 , pp. 483-487
    • Penkova, R.1    Goshev, I.2    Gorinstein, S.3    Nedkov, P.4
  • 34
    • 0023046618 scopus 로고
    • Interaction of calf skin collagen with glycerol: Linked function analysis
    • G.C. Na Interaction of calf skin collagen with glycerol: linked function analysis Biochemistry 25 1986 967 973
    • (1986) Biochemistry , vol.25 , pp. 967-973
    • Na, G.C.1
  • 35
    • 72749102457 scopus 로고    scopus 로고
    • Mechanisms of protein stabilization and prevention of protein aggregation by glycerol
    • V. Vagenende, M.G.S. Yap, and B.L. Trout Mechanisms of protein stabilization and prevention of protein aggregation by glycerol Biochemistry 48 2009 11084 11096
    • (2009) Biochemistry , vol.48 , pp. 11084-11096
    • Vagenende, V.1    Yap, M.G.S.2    Trout, B.L.3
  • 36
    • 84987284112 scopus 로고
    • Some stereochemical implications of the molecular comformation of collagen
    • W. Traub Some stereochemical implications of the molecular comformation of collagen Isr. J. Chem. 12 1974 435 439
    • (1974) Isr. J. Chem. , vol.12 , pp. 435-439
    • Traub, W.1
  • 37
    • 0015852842 scopus 로고
    • A hypothesis on the role of hydroxyproline in stabilizaing collagen structure
    • G.N. Ramachandran, M. Bansal, and R.S. Bhatnagar A hypothesis on the role of hydroxyproline in stabilizaing collagen structure Biochim. Biophys. Acta 322 1973 166 171
    • (1973) Biochim. Biophys. Acta , vol.322 , pp. 166-171
    • Ramachandran, G.N.1    Bansal, M.2    Bhatnagar, R.S.3
  • 38
    • 0018400235 scopus 로고
    • Chain conformation in the collagen molecule
    • DOI 10.1016/0022-2836(79)90507-2
    • R.D.B. Fraser, T.P. McRae, and E. Suzuki Chain conformation in the collagen molecule J. Mol. Biol. 129 1979 463 481 (Pubitemid 9168804)
    • (1979) Journal of Molecular Biology , vol.129 , Issue.3 , pp. 463-481
    • Fraser, R.D.B.1    MacRae, T.P.2    Suzuki, E.3
  • 39
    • 0034693136 scopus 로고    scopus 로고
    • Identification of an intermediate state in the helix-coil degradation of collagen by ultraviolet light
    • C.A. Miles, A. Sionkowska, S.L. Hulin, T.J. Sims, N.C. Avery, and A.J. Bailey Identification of an intermediate state in the helix-coil degradation of collagen by ultraviolet light J. Biol. Chem. 275 2000 33014 33020
    • (2000) J. Biol. Chem. , vol.275 , pp. 33014-33020
    • Miles, C.A.1    Sionkowska, A.2    Hulin, S.L.3    Sims, T.J.4    Avery, N.C.5    Bailey, A.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.