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Volumn 105, Issue 7, 2013, Pages 1681-1688

The role of cross-chain ionic interactions for the stability of collagen model peptides

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN;

EID: 84885108705     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.08.018     Document Type: Article
Times cited : (27)

References (37)
  • 2
    • 13444292142 scopus 로고    scopus 로고
    • Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability
    • A.V. Persikov, and J.A.M. Ramshaw B. Brodsky 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    Brodsky, B.3
  • 3
    • 84858050116 scopus 로고    scopus 로고
    • Structural insights into charge pair interactions in triple helical collagen-like proteins
    • J.A. Fallas, and J. Dong J.D. Hartgerink Structural insights into charge pair interactions in triple helical collagen-like proteins J. Biol. Chem. 287 2012 8039 8047
    • (2012) J. Biol. Chem. , vol.287 , pp. 8039-8047
    • Fallas, J.A.1    Dong, J.2    Hartgerink, J.D.3
  • 4
    • 70350353198 scopus 로고    scopus 로고
    • Solution structure of an ABC collagen heterotrimer reveals a single-register helix stabilized by electrostatic interactions
    • J.A. Fallas, V. Gauba, and J.D. Hartgerink Solution structure of an ABC collagen heterotrimer reveals a single-register helix stabilized by electrostatic interactions J. Biol. Chem. 284 2009 26851 26859
    • (2009) J. Biol. Chem. , vol.284 , pp. 26851-26859
    • Fallas, J.A.1    Gauba, V.2    Hartgerink, J.D.3
  • 5
    • 36849062200 scopus 로고    scopus 로고
    • Surprisingly high stability of collagen ABC heterotrimer: Evaluation of side chain charge pairs
    • V. Gauba, and J.D. Hartgerink Surprisingly high stability of collagen ABC heterotrimer: evaluation of side chain charge pairs J. Am. Chem. Soc. 129 2007 15034 15041
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15034-15041
    • Gauba, V.1    Hartgerink, J.D.2
  • 6
    • 0028261035 scopus 로고
    • Electrostatic interactions in collagen-like triple-helical peptides
    • M.G. Venugopal, and J.A. Ramshaw B. Brodsky Electrostatic interactions in collagen-like triple-helical peptides Biochemistry 33 1994 7948 7956
    • (1994) Biochemistry , vol.33 , pp. 7948-7956
    • Venugopal, M.G.1    Ramshaw, J.A.2    Brodsky, B.3
  • 7
    • 21444453832 scopus 로고    scopus 로고
    • Prediction of collagen stability from amino acid sequence
    • A.V. Persikov, J.A.M. Ramshaw, and B. Brodsky Prediction of collagen stability from amino acid sequence J. Biol. Chem. 280 2005 19343 19349
    • (2005) J. Biol. Chem. , vol.280 , pp. 19343-19349
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Brodsky, B.3
  • 8
    • 84886751814 scopus 로고    scopus 로고
    • Rules derived from host-guest peptides allow prediction of triple-helix stability
    • A.V. Persikov, J. Ramshaw, and B. Brodsky Rules derived from host-guest peptides allow prediction of triple-helix stability Biophys. J. 88 2005 560a
    • (2005) Biophys. J. , vol.88
    • Persikov, A.V.1    Ramshaw, J.2    Brodsky, B.3
  • 9
    • 84886752656 scopus 로고    scopus 로고
    • Amino-acid pairwise interactions in collagen triple-helix
    • A.V. Persikov, and A. Kirkpatrick B. Brodsky Amino-acid pairwise interactions in collagen triple-helix Biophys. J. 82 2002 294a
    • (2002) Biophys. J. , vol.82
    • Persikov, A.V.1    Kirkpatrick, A.2    Brodsky, B.3
  • 10
    • 0034610308 scopus 로고    scopus 로고
    • Amino acid propensities for the collagen triple-helix
    • A.V. Persikov, and J.A.M. Ramshaw B. Brodsky Amino acid propensities for the collagen triple-helix Biochemistry 39 2000 14960 14967
    • (2000) Biochemistry , vol.39 , pp. 14960-14967
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Brodsky, B.3
  • 11
    • 0034442555 scopus 로고    scopus 로고
    • Collagen model peptides: Sequence dependence of triple-helix stability
    • A.V. Persikov, J.A.M. Ramshaw, and B. Brodsky 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.M.2    Brodsky, B.3
  • 12
    • 0031692464 scopus 로고    scopus 로고
    • Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides
    • J.A.M. Ramshaw, N.K. Shah, and B. Brodsky Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides J. Struct. Biol. 122 1998 86 91
    • (1998) J. Struct. Biol. , vol.122 , pp. 86-91
    • Ramshaw, J.A.M.1    Shah, N.K.2    Brodsky, B.3
  • 13
    • 0016669438 scopus 로고
    • Conformational implications of amino acid sequence regularities in collagen
    • G. Salem, and W. Traub Conformational implications of amino acid sequence regularities in collagen FEBS Lett. 51 1975 94 99
    • (1975) FEBS Lett. , vol.51 , pp. 94-99
    • Salem, G.1    Traub, W.2
  • 14
    • 0036298978 scopus 로고    scopus 로고
    • Peptide investigations of pairwise interactions in the collagen triple-helix
    • A.V. Persikov, and J.A.M. Ramshaw B. Brodsky Peptide investigations of pairwise interactions in the collagen triple-helix J. Mol. Biol. 316 2002 385 394
    • (2002) J. Mol. Biol. , vol.316 , pp. 385-394
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Brodsky, B.3
  • 15
    • 0034283338 scopus 로고    scopus 로고
    • Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair
    • R.Z. Kramer, and M.G. Venugopal H.M. Berman Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair J. Mol. Biol. 301 2000 1191 1205
    • (2000) J. Mol. Biol. , vol.301 , pp. 1191-1205
    • Kramer, R.Z.1    Venugopal, M.G.2    Berman, H.M.3
  • 16
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • W.L. Jorgensen, and J. Chandrasekhar M.L. Klein Comparison of simple potential functions for simulating liquid water J. Chem. Phys. 79 1983 926 935
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 17
    • 0000020246 scopus 로고    scopus 로고
    • A five-site model for liquid water and the reproduction of the density anomaly by rigid, nonpolarizable potential functions
    • M.W. Mahoney, and W.L. Jorgensen A five-site model for liquid water and the reproduction of the density anomaly by rigid, nonpolarizable potential functions J. Chem. Phys. 112 2000 8910 8922
    • (2000) J. Chem. Phys. , vol.112 , pp. 8910-8922
    • Mahoney, M.W.1    Jorgensen, W.L.2
  • 18
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • V. Hornak, and R. Abel C. Simmerling Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins 65 2006 712 725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Simmerling, C.3
  • 19
    • 84943502952 scopus 로고
    • A molecular-dynamics method for simulations in the canonical ensemble
    • S. Nose A molecular-dynamics method for simulations in the canonical ensemble Mol. Phys. 52 1984 255 268
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nose, S.1
  • 20
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 31 1985 1695 1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 21
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals - A new molecular dynamics method
    • M. Parrinello, and A. Rahman Polymorphic transitions in single crystals - a new molecular dynamics method J. Appl. Phys. 52 1981 7182 7190
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 22
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • S. Nose, and M.L. Klein Constant pressure molecular dynamics for molecular systems Mol. Phys. 50 1983 1055 1076
    • (1983) Mol. Phys. , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.L.2
  • 24
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • K. Lindorff-Larsen, and S. Piana D.E. Shaw Improved side-chain torsion potentials for the Amber ff99SB protein force field Proteins 78 2010 1950 1958
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1    Piana, S.2    Shaw, D.E.3
  • 25
    • 1842559515 scopus 로고    scopus 로고
    • Equilibrium thermal transitions of collagen model peptides
    • A.V. Persikov, Y.J. Xu, and B. Brodsky Equilibrium thermal transitions of collagen model peptides Protein Sci. 13 2004 893 902
    • (2004) Protein Sci. , vol.13 , pp. 893-902
    • Persikov, A.V.1    Xu, Y.J.2    Brodsky, B.3
  • 26
    • 79958769952 scopus 로고    scopus 로고
    • Statistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges
    • J. Bush, and G.I. Makhatadze Statistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges Proteins 79 2011 2027 2032
    • (2011) Proteins , vol.79 , pp. 2027-2032
    • Bush, J.1    Makhatadze, G.I.2
  • 27
    • 81055140446 scopus 로고    scopus 로고
    • Energetics of charge-charge interactions between residues adjacent in sequence
    • V.V. Loladze, and G.I. Makhatadze Energetics of charge-charge interactions between residues adjacent in sequence Proteins 79 2011 3494 3499
    • (2011) Proteins , vol.79 , pp. 3494-3499
    • Loladze, V.V.1    Makhatadze, G.I.2
  • 28
    • 0037432563 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability: Guidelines for protein engineering
    • G.I. Makhatadze, and V.V. Loladze S.T. Thomas Contribution of surface salt bridges to protein stability: guidelines for protein engineering J. Mol. Biol. 327 2003 1135 1148
    • (2003) J. Mol. Biol. , vol.327 , pp. 1135-1148
    • Makhatadze, G.I.1    Loladze, V.V.2    Thomas, S.T.3
  • 30
    • 0021763134 scopus 로고
    • On the environment of ionizable groups in globular proteins
    • A.A. Rashin, and B. Honig On the environment of ionizable groups in globular proteins J. Mol. Biol. 173 1984 515 521
    • (1984) J. Mol. Biol. , vol.173 , pp. 515-521
    • Rashin, A.A.1    Honig, B.2
  • 32
    • 0033583066 scopus 로고    scopus 로고
    • Sequence dependence of the folding of collagen-like peptides. Single amino acids affect the rate of triple-helix nucleation
    • M.S. Ackerman, and M. Bhate B. Brodsky Sequence dependence of the folding of collagen-like peptides. Single amino acids affect the rate of triple-helix nucleation J. Biol. Chem. 274 1999 7668 7673
    • (1999) J. Biol. Chem. , vol.274 , pp. 7668-7673
    • Ackerman, M.S.1    Bhate, M.2    Brodsky, B.3
  • 33
    • 77952994823 scopus 로고    scopus 로고
    • The contribution of interchain salt bridges to triple-helical stability in collagen
    • T. Gurry, P.S. Nerenberg, and C.M. Stultz The contribution of interchain salt bridges to triple-helical stability in collagen Biophys. J. 98 2010 2634 2643
    • (2010) Biophys. J. , vol.98 , pp. 2634-2643
    • Gurry, T.1    Nerenberg, P.S.2    Stultz, C.M.3
  • 34
    • 80455129245 scopus 로고    scopus 로고
    • Influence of water-protein hydrogen bonding on the stability of Trp-cage miniprotein. A comparison between the TIP3P and TIP4P-Ew water models
    • D. Paschek, R. Day, and A.E. García Influence of water-protein hydrogen bonding on the stability of Trp-cage miniprotein. A comparison between the TIP3P and TIP4P-Ew water models Phys. Chem. Chem. Phys. 13 2011 19840 19847
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 19840-19847
    • Paschek, D.1    Day, R.2    García, A.E.3
  • 35
    • 77749285768 scopus 로고    scopus 로고
    • Equilibrium study of protein denaturation by urea
    • D.R. Canchi, D. Paschek, and A.E. García Equilibrium study of protein denaturation by urea J. Am. Chem. Soc. 132 2010 2338 2344
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2338-2344
    • Canchi, D.R.1    Paschek, D.2    García, A.E.3
  • 36
    • 56649083699 scopus 로고    scopus 로고
    • Computing the stability diagram of the Trp-cage miniprotein
    • D. Paschek, S. Hempel, and A.E. García Computing the stability diagram of the Trp-cage miniprotein Proc. Natl. Acad. Sci. USA 105 2008 17754 17759
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17754-17759
    • Paschek, D.1    Hempel, S.2    García, A.E.3
  • 37
    • 80053253228 scopus 로고    scopus 로고
    • Protonation/deprotonation effects on the stability of the Trp-cage miniprotein
    • C.A. Jimenez-Cruz, G.I. Makhatadze, and A.E. Garcia Protonation/ deprotonation effects on the stability of the Trp-cage miniprotein Phys. Chem. Chem. Phys. 13 2011 17056 17063
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 17056-17063
    • Jimenez-Cruz, C.A.1    Makhatadze, G.I.2    Garcia, A.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.