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Volumn 53, Issue 20, 2005, Pages 7802-7806

Effect of deamidation on stability for the collagen to gelatin transition

Author keywords

Collagen; Deamidation; Gelatin; Peptide models; Thermal stability; Triple helix

Indexed keywords

AMIDE; ASPARAGINE; COLLAGEN; GELATIN; GLUTAMINE; PEPTIDE;

EID: 27144507339     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf050944d     Document Type: Article
Times cited : (20)

References (23)
  • 1
    • 0018400235 scopus 로고
    • Chain conformation in the collagen molecule
    • Fraser, R. D. B.; MacRae, T. P.; Suzuki, E. Chain conformation in the collagen molecule. J. Mol. Biol. 1979, 129, 463-481.
    • (1979) J. Mol. Biol. , vol.129 , pp. 463-481
    • Fraser, R.D.B.1    MacRae, T.P.2    Suzuki, E.3
  • 2
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
    • Bella, J.; Eaton, M.; Brodsky, B.; Berman, H. M. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science 1994, 266, 75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 3
    • 0030963588 scopus 로고    scopus 로고
    • The collagen triple-helix structure
    • Brodsky, B.; Ramshaw, J. A. M. The collagen triple-helix structure. Matrix Biol. 1997, 15, 545-554.
    • (1997) Matrix Biol. , vol.15 , pp. 545-554
    • Brodsky, B.1    Ramshaw, J.A.M.2
  • 5
    • 85053589021 scopus 로고
    • Cross-linking of collagen
    • Nimni, M. E., Ed.; CRC Press: Boca Raton, FL
    • Yamauchi, M.; Mechanic, G. L. Cross-linking of collagen. In Collagen; Nimni, M. E., Ed.; CRC Press: Boca Raton, FL, 1988; Vol. 1, pp 157-172.
    • (1988) Collagen , vol.1 , pp. 157-172
    • Yamauchi, M.1    Mechanic, G.L.2
  • 6
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence crosslink from human extracellular matrix: Implication of pentoses in aging process
    • Sell, D. R.; Monier, V. M. Structure elucidation of a senescence crosslink from human extracellular matrix: implication of pentoses in aging process. J. Biol. Chem. 1989, 264, 21597-21602.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monier, V.M.2
  • 7
    • 0029760932 scopus 로고    scopus 로고
    • Isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal
    • Nagaraj, R. H.; Shipanova, I. N.; Faust, F. M. Isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal. J. Biol. Chem. 1996, 271, 19338-19345.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19338-19345
    • Nagaraj, R.H.1    Shipanova, I.N.2    Faust, F.M.3
  • 9
    • 27144489942 scopus 로고    scopus 로고
    • Molecular structure of gelatine gels
    • Aalbersberg, W. Y., Hamers, R. J., Jasperse, P., de Jong, H. H. J., de Kruif, C. G., Walstra, P., de Wolf, F. A., Eds.; Elsevier: Amsterdam, The Netherlands, Chapter 5, Section 2.1
    • de Wolf, F. A. Molecular structure of gelatine gels. In Industrial Proteins in Perspective, Progress in Biotechnology; Aalbersberg, W. Y., Hamers, R. J., Jasperse, P., de Jong, H. H. J., de Kruif, C. G., Walstra, P., de Wolf, F. A., Eds.; Elsevier: Amsterdam, The Netherlands, 2003; Chapter 5, Section 2.1, pp 159-167.
    • (2003) Industrial Proteins in Perspective, Progress in Biotechnology , pp. 159-167
    • De Wolf, F.A.1
  • 10
    • 27144495182 scopus 로고    scopus 로고
    • Gelatin extraction. U.S. Patent 4,-064,008, 1977
    • Petersen, B. R.; Yates, J. R. Gelatin extraction. U.S. Patent 4,-064,008, 1977.
    • Petersen, B.R.1    Yates, J.R.2
  • 11
    • 0022594310 scopus 로고
    • Distribution of type III collagen in bovine skin of various ages
    • Ramshaw, J. A. M. Distribution of type III collagen in bovine skin of various ages. Connect. Tissue Res. 1986, 14, 307-314.
    • (1986) Connect. Tissue Res. , vol.14 , pp. 307-314
    • Ramshaw, J.A.M.1
  • 12
    • 0016369726 scopus 로고
    • Gel chromatography studies of gelatin
    • Coopes, I. Gel chromatography studies of gelatin J. Polym. Sci. 1975, 49, 97-107.
    • (1975) J. Polym. Sci. , vol.49 , pp. 97-107
    • Coopes, I.1
  • 13
    • 0036298978 scopus 로고    scopus 로고
    • Peptide investigations of side chain interactions in the collagen triple-helix
    • Persikov, A. V.; Ramshaw, J. A. M.; Kirkpatrick, A.; Brodsky, B. Peptide investigations of side chain interactions in the collagen triple-helix. J. Mol. Biol. 2002, 316, 385-394.
    • (2002) J. Mol. Biol. , vol.316 , pp. 385-394
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Kirkpatrick, A.3    Brodsky, B.4
  • 14
    • 0031465742 scopus 로고    scopus 로고
    • Positional preferences of ionizable residues in Gly-X-Y triplets of the collagen triple-helix
    • Chan, V. C.; Ramshaw, J. A. M.; Kirkpatrick, A.; Beck, K.; Brodsky, B. Positional preferences of ionizable residues in Gly-X-Y triplets of the collagen triple-helix. J. Biol. Chem. 1997, 272, 31441-31446.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31441-31446
    • Chan, V.C.1    Ramshaw, J.A.M.2    Kirkpatrick, A.3    Beck, K.4    Brodsky, B.5
  • 16
    • 0020010851 scopus 로고
    • Preparation and characterisation of the different types of collagens
    • Miller, E. J.; Rhodes, R. K. Preparation and characterisation of the different types of collagens. Methods Enzymol. 1982, 82, 33-64.
    • (1982) Methods Enzymol. , vol.82 , pp. 33-64
    • Miller, E.J.1    Rhodes, R.K.2
  • 17
    • 0014280515 scopus 로고
    • The renaturation behaviour of modified collagen molecules
    • Rauterberg, J.; Kuhn, K. The renaturation behaviour of modified collagen molecules. Hoppe-Seyler's Z. Physiol. Chem. 1968, 349, 611-622.
    • (1968) Hoppe-Seyler's Z. Physiol. Chem. , vol.349 , pp. 611-622
    • Rauterberg, J.1    Kuhn, K.2
  • 19
    • 0033526117 scopus 로고    scopus 로고
    • Structural consequences of D-amino acids in collagen triple-helical peptides
    • Shah, N. K.; Brodsky, B.; Kirkpatrick, A.; Ramshaw, J. A. M. Structural consequences of D-amino acids in collagen triple-helical peptides. Biopolymers 1999, 49, 297-302.
    • (1999) Biopolymers , vol.49 , pp. 297-302
    • Shah, N.K.1    Brodsky, B.2    Kirkpatrick, A.3    Ramshaw, J.A.M.4
  • 20
    • 0031692464 scopus 로고    scopus 로고
    • Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides
    • Ramshaw, J. A. M.; Shah, N. K.; Brodsky, B. Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. J. Struct. Biol. 1998, 122, 86-91.
    • (1998) J. Struct. Biol. , vol.122 , pp. 86-91
    • Ramshaw, J.A.M.1    Shah, N.K.2    Brodsky, B.3
  • 21
    • 0028679665 scopus 로고
    • Extracellular matrix. 1. Fibril forming collagens
    • Kadler, K. Extracellular matrix. 1. Fibril forming collagens. Protein Profile 1994, 1, 519-638.
    • (1994) Protein Profile , vol.1 , pp. 519-638
    • Kadler, K.1
  • 23
    • 13444292142 scopus 로고    scopus 로고
    • Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability
    • Persikov, A. V.; Ramshaw, J. A. M.; Kirkpatrick, A.; Brodsky, B. Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability. Biochemistry 2005, 44, 1414-1422.
    • (2005) Biochemistry , vol.44 , pp. 1414-1422
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Kirkpatrick, A.3    Brodsky, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.