메뉴 건너뛰기




Volumn 41, Issue 14, 2008, Pages 3073-3077

Mechanical properties of physiological and pathological models of collagen peptides investigated via steered molecular dynamics simulations

Author keywords

Collagen; Disease associated mutation; Mechanical properties; Molecular modelling; Osteogenesis imperfecta

Indexed keywords

AMINES; COLLAGEN; DYNAMICS; ELASTIC MODULI; ELASTICITY; HYDROGEN; HYDROGEN BONDS; HYDROPHOBICITY; MECHANICAL PROPERTIES; MOLECULAR DYNAMICS; PEPTIDES; PROTEINS; QUANTUM CHEMISTRY;

EID: 53149100799     PISSN: 00219290     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiomech.2008.06.028     Document Type: Article
Times cited : (50)

References (29)
  • 1
    • 0034636101 scopus 로고    scopus 로고
    • Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine
    • Beck K., Chan V.C., and Shenoy N. Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine. Proceedings of the National Academy of Science 97 (2000) 4273-4278
    • (2000) Proceedings of the National Academy of Science , vol.97 , pp. 4273-4278
    • Beck, K.1    Chan, V.C.2    Shenoy, N.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., and Berman H.M. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science 266 (1994) 75-81
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 4
    • 0034424953 scopus 로고    scopus 로고
    • Crystal structure of a collagen-like polypeptide with repeating sequence Pro-Hyp-Gly at 1.4 Å resolution: implications for collagen hydration
    • Berisio R., Vitagliano L., Mozzarella L., and Zagari A. Crystal structure of a collagen-like polypeptide with repeating sequence Pro-Hyp-Gly at 1.4 Å resolution: implications for collagen hydration. Biopolymers 56 (2001) 8-13
    • (2001) Biopolymers , vol.56 , pp. 8-13
    • Berisio, R.1    Vitagliano, L.2    Mozzarella, L.3    Zagari, A.4
  • 5
    • 33747630320 scopus 로고    scopus 로고
    • Atomistic and continuum modelling of mechanical properties of collagen: elasticity, fracture and self-assembly
    • Buehler M.J. Atomistic and continuum modelling of mechanical properties of collagen: elasticity, fracture and self-assembly. Journal of Material Research 21 (2006) 1947-1961
    • (2006) Journal of Material Research , vol.21 , pp. 1947-1961
    • Buehler, M.J.1
  • 6
    • 0033819621 scopus 로고    scopus 로고
    • Collagens: building blocks at the end of the development line
    • Byers P.H. Collagens: building blocks at the end of the development line. Clinical Genetics 58 (2000) 270-279
    • (2000) Clinical Genetics , vol.58 , pp. 270-279
    • Byers, P.H.1
  • 8
    • 0018566616 scopus 로고
    • Determination of the elastic constants of collagen by Brillouin light scattering
    • Cusack S., and Miller A. Determination of the elastic constants of collagen by Brillouin light scattering. Journal of Molecular Biology 135 (1979) 39-51
    • (1979) Journal of Molecular Biology , vol.135 , pp. 39-51
    • Cusack, S.1    Miller, A.2
  • 9
    • 0030789557 scopus 로고    scopus 로고
    • The human type I collagen mutation database
    • Dalgleish R. The human type I collagen mutation database. Nucleic Acids Research 25 (1997) 181-187
    • (1997) Nucleic Acids Research , vol.25 , pp. 181-187
    • Dalgleish, R.1
  • 10
    • 0034737296 scopus 로고    scopus 로고
    • Structural basis of collagen recognition by integrin α2β1
    • Emsley J., Knight C.G., Farndale R.W., and Barnes M.J. Structural basis of collagen recognition by integrin α2β1. Cell 101 (2000) 47-56
    • (2000) Cell , vol.101 , pp. 47-56
    • Emsley, J.1    Knight, C.G.2    Farndale, R.W.3    Barnes, M.J.4
  • 12
    • 0017390580 scopus 로고
    • Phonons and the elastic moduli of collagen and muscle
    • Harley R., James D., Miller A., and White J.W. Phonons and the elastic moduli of collagen and muscle. Nature 267 (1977) 285-287
    • (1977) Nature , vol.267 , pp. 285-287
    • Harley, R.1    James, D.2    Miller, A.3    White, J.W.4
  • 13
    • 0021770213 scopus 로고
    • Localization of flexible sites in thread-like molecules from electron micrographs. Comparison of interstitial, basement membrane and intima collagens
    • Hofmann H., Voss T., Kuhn K., and Engel J. Localization of flexible sites in thread-like molecules from electron micrographs. Comparison of interstitial, basement membrane and intima collagens. Journal of Molecular Biology 172 (1984) 325-343
    • (1984) Journal of Molecular Biology , vol.172 , pp. 325-343
    • Hofmann, H.1    Voss, T.2    Kuhn, K.3    Engel, J.4
  • 14
    • 0036007873 scopus 로고    scopus 로고
    • Insights on the conformational stability of collagen
    • Jenkins C.L., and Raines R.T. Insights on the conformational stability of collagen. Natural Products Report 19 (2002) 49-59
    • (2002) Natural Products Report , vol.19 , pp. 49-59
    • Jenkins, C.L.1    Raines, R.T.2
  • 16
    • 0034283338 scopus 로고    scopus 로고
    • Crystal structure of the triple-helical collagen-like peptide, (Pro-Hyp-Gly)4-Glu-Lys-Gly(Pro-Hyp-Gly)5
    • Kramer R.Z., Venugopal M., and Bella J. Crystal structure of the triple-helical collagen-like peptide, (Pro-Hyp-Gly)4-Glu-Lys-Gly(Pro-Hyp-Gly)5. Journal of Molecular Biology 301 (2000) 1191-1205
    • (2000) Journal of Molecular Biology , vol.301 , pp. 1191-1205
    • Kramer, R.Z.1    Venugopal, M.2    Bella, J.3
  • 17
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., and Van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. Journal of Molecular Modeling 7 8 (2001) 306-317
    • (2001) Journal of Molecular Modeling , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van der Spoel, D.3
  • 18
    • 19744370421 scopus 로고    scopus 로고
    • Elastic properties, Young's modulus determination and structural stability of the tropocollagen molecule: a computational study by steered molecular dynamics
    • Lorenzo A.C., and Caffarena E.R. Elastic properties, Young's modulus determination and structural stability of the tropocollagen molecule: a computational study by steered molecular dynamics. Journal of Biomechanics 38 (2005) 1527-1533
    • (2005) Journal of Biomechanics , vol.38 , pp. 1527-1533
    • Lorenzo, A.C.1    Caffarena, E.R.2
  • 19
    • 0035984335 scopus 로고    scopus 로고
    • The role of the α2 chain in the stabilization of the collagen type I heterotrimer: a study of the type I homotrimer in oim mouse tissues
    • Miles C.A., Sims T.J., Camacho N.P., and Bailey A.J. The role of the α2 chain in the stabilization of the collagen type I heterotrimer: a study of the type I homotrimer in oim mouse tissues. Journal of Molecular Biology 321 (2002) 797-805
    • (2002) Journal of Molecular Biology , vol.321 , pp. 797-805
    • Miles, C.A.1    Sims, T.J.2    Camacho, N.P.3    Bailey, A.J.4
  • 21
    • 2342518375 scopus 로고    scopus 로고
    • Structural models of osteogenesis imperfecta-associated variants in the COL1A1 gene
    • Mooney S.D., and Klein T.E. Structural models of osteogenesis imperfecta-associated variants in the COL1A1 gene. Molecular and Cellular Proteomics 1 (2002) 868-875
    • (2002) Molecular and Cellular Proteomics , vol.1 , pp. 868-875
    • Mooney, S.D.1    Klein, T.E.2
  • 22
    • 0034442555 scopus 로고    scopus 로고
    • Collagen model peptides: sequence dependence of triple-helix stability
    • Persikov A.V., Ramshaw J.A., and Brodsky B. Collagen model peptides: sequence dependence of triple-helix stability. Biopolymers 55 (2000) 436-450
    • (2000) Biopolymers , vol.55 , pp. 436-450
    • Persikov, A.V.1    Ramshaw, J.A.2    Brodsky, B.3
  • 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., and Brodsky B. Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability. Biochemistry 44 (2005) 1414-1422
    • (2005) Biochemistry , vol.44 , pp. 1414-1422
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Kirkpatrick, A.3    Brodsky, B.4
  • 24
    • 7244253096 scopus 로고    scopus 로고
    • An interactive triple-helical collagen builder
    • Rainey J.K., and Goh M.C. An interactive triple-helical collagen builder. Bioinformatics 20 (2004) 2458-2459
    • (2004) Bioinformatics , vol.20 , pp. 2458-2459
    • Rainey, J.K.1    Goh, M.C.2
  • 26
    • 0030152813 scopus 로고    scopus 로고
    • Stress-strain curve and Young's modulus of a collagen molecule as determined by the X-ray diffraction technique
    • Sasaki N., and Odajima S. Stress-strain curve and Young's modulus of a collagen molecule as determined by the X-ray diffraction technique. Journal of Biomechanics 29 (1996) 655-658
    • (1996) Journal of Biomechanics , vol.29 , pp. 655-658
    • Sasaki, N.1    Odajima, S.2
  • 29
    • 0028904399 scopus 로고
    • Structure of the type I collagen molecule based on conformational energy computations: the triple-stranded helix and the N-terminal telopeptide
    • Vitagliano L., Nemethy G., Zagari A., and Scherana H.A. Structure of the type I collagen molecule based on conformational energy computations: the triple-stranded helix and the N-terminal telopeptide. Journal of Molecular Biology 247 (1995) 69-80
    • (1995) Journal of Molecular Biology , vol.247 , pp. 69-80
    • Vitagliano, L.1    Nemethy, G.2    Zagari, A.3    Scherana, H.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.