메뉴 건너뛰기




Volumn 1702, Issue 1, 2004, Pages 1-8

Charge sequence coding in statistical modeling of unfolded proteins

Author keywords

Charge sequence; Statistical; Unfolded protein

Indexed keywords

DROSOPHILA PROTEIN; POLYPEPTIDE; PROTEIN DRK; UNCLASSIFIED DRUG;

EID: 4644306055     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.07.001     Document Type: Article
Times cited : (8)

References (24)
  • 1
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure - Function paradigm
    • P.E. Wright, and H.J. Dyson Intrinsically unstructured proteins: re-assessing the protein structure - function paradigm J. Mol. Biol. 293 1999 321 331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 2
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • V.N. Uversky Natively unfolded proteins: a point where biology waits for physics Protein Sci. 11 2002 739 756
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 4
    • 0036081435 scopus 로고    scopus 로고
    • Modeling of denatured state for calculation of the electrostatic contribution to protein stability
    • P.J. Kundrotas, and A. Karshikoff Modeling of denatured state for calculation of the electrostatic contribution to protein stability Protein Sci. 11 2002 1681 1686
    • (2002) Protein Sci. , vol.11 , pp. 1681-1686
    • Kundrotas, P.J.1    Karshikoff, A.2
  • 5
    • 0028305457 scopus 로고
    • Prediction of pH-dependent properties of proteins
    • J. Antosiewicz, J.A. McCammon, and M.K. Gilson Prediction of pH-dependent properties of proteins J. Mol. Biol. 238 1994 415 436
    • (1994) J. Mol. Biol. , vol.238 , pp. 415-436
    • Antosiewicz, J.1    McCammon, J.A.2    Gilson, M.K.3
  • 6
    • 0037294839 scopus 로고    scopus 로고
    • PH-dependent stability of Sperm whale myoglobin in water - Guanidine hydrochloride solutions
    • A. Shosheva, M. Miteva, P. Christova, and B. Atanasov pH-dependent stability of Sperm whale myoglobin in water - guanidine hydrochloride solutions Eur. Biophys. J. 31 2003 617 625
    • (2003) Eur. Biophys. J. , vol.31 , pp. 617-625
    • Shosheva, A.1    Miteva, M.2    Christova, P.3    Atanasov, B.4
  • 7
    • 0031076776 scopus 로고    scopus 로고
    • PH-dependence of protein stability: Absolute electrostatic free energy differences between conformations
    • M. Schaefer, M. Sommer, and M. Karplus pH-dependence of protein stability: absolute electrostatic free energy differences between conformations J. Phys. Chem. B 101 1997 1663 1683
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1663-1683
    • Schaefer, M.1    Sommer, M.2    Karplus, M.3
  • 8
    • 0032586777 scopus 로고    scopus 로고
    • Simplified methods for pK(a) and acid pH-dependent stability estimation in proteins: Removing dielectric and counterion boundaries
    • J. Warwicker Simplified methods for pK(a) and acid pH-dependent stability estimation in proteins: removing dielectric and counterion boundaries Protein Sci. 8 1999 418 425
    • (1999) Protein Sci. , vol.8 , pp. 418-425
    • Warwicker, J.1
  • 9
    • 0033544710 scopus 로고    scopus 로고
    • Realistic modeling of the denatured states of proteins allows accurate calculations of the pH dependence of protein stability
    • A.H. Elcock Realistic modeling of the denatured states of proteins allows accurate calculations of the pH dependence of protein stability J. Mol. Biol. 294 1999 1051 1062
    • (1999) J. Mol. Biol. , vol.294 , pp. 1051-1062
    • Elcock, A.H.1
  • 10
    • 41349115238 scopus 로고    scopus 로고
    • Model for calculation of electrostatic interactions in unfolded proteins
    • P.J. Kundrotas, and A. Karshikoff Model for calculation of electrostatic interactions in unfolded proteins Phys. Rev., E 6501 2002 (art. no. 011901)
    • (2002) Phys. Rev., e , vol.6501
    • Kundrotas, P.J.1    Karshikoff, A.2
  • 11
    • 0037150077 scopus 로고    scopus 로고
    • Residual electrostatic effects in the unfolded state of the N-terminal domain of L9 can be attributed to nonspecific nonlocal charge - Charge interactions
    • H.X. Zhou Residual electrostatic effects in the unfolded state of the N-terminal domain of L9 can be attributed to nonspecific nonlocal charge - charge interactions Biochemistry 41 2002 6533 6538
    • (2002) Biochemistry , vol.41 , pp. 6533-6538
    • Zhou, H.X.1
  • 12
    • 0037133605 scopus 로고    scopus 로고
    • A Gaussian-chain model for treating residual charge - Charge interactions in the unfolded state of proteins
    • H.X. Zhou A Gaussian-chain model for treating residual charge - charge interactions in the unfolded state of proteins Proc. Natl. Acad. Sci. U. S. A. 99 2002 3569 3574
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3569-3574
    • Zhou, H.X.1
  • 13
    • 0037467111 scopus 로고    scopus 로고
    • Direct test of the Gaussian-chain model for treating residual charge - Charge interactions in the unfolded state of proteins
    • H.X. Zhou Direct test of the Gaussian-chain model for treating residual charge - Charge interactions in the unfolded state of proteins J. Am. Chem. Soc. 125 2003 2060 2061
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2060-2061
    • Zhou, H.X.1
  • 14
    • 0041878652 scopus 로고    scopus 로고
    • Effects of charge - charge interactions on dimensions of unfolded proteins: A Monte Carlo study
    • P.J. Kundrotas, and A. Karshikoff Effects of charge - charge interactions on dimensions of unfolded proteins: a Monte Carlo study J. Chem. Phys. 119 2003 3574 3581
    • (2003) J. Chem. Phys. , vol.119 , pp. 3574-3581
    • Kundrotas, P.J.1    Karshikoff, A.2
  • 15
    • 0037157124 scopus 로고    scopus 로고
    • Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy
    • M. Tollinger, J.D. Forman-Kay, and L.E. Kay Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy J. Am. Chem. Soc. 124 2002 5714 5717
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5714-5717
    • Tollinger, M.1    Forman-Kay, J.D.2    Kay, L.E.3
  • 19
    • 1542364450 scopus 로고    scopus 로고
    • Structure of human microsomal cytochrome P4502C8 - Evidence for a peripheral fatty acid binding site
    • G.A. Schoch, J.K. Yano, M.R. Wester, K.J. Griffin, C.D. Stout, and E.F. Johnson Structure of human microsomal cytochrome P4502C8 - evidence for a peripheral fatty acid binding site J. Biol. Chem. 279 2004 9497 9503
    • (2004) J. Biol. Chem. , vol.279 , pp. 9497-9503
    • Schoch, G.A.1    Yano, J.K.2    Wester, M.R.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 20
    • 0032836911 scopus 로고    scopus 로고
    • Human replication protein A: Global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker
    • D.M. Jacobs, A.S. Lipton, N.G. Isern, G.W. Daughdrill, D.F. Lowry, X. Gomes, and M.S. Wold Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker J. Biomol. NMR 14 1999 321 331
    • (1999) J. Biomol. NMR , vol.14 , pp. 321-331
    • Jacobs, D.M.1    Lipton, A.S.2    Isern, N.G.3    Daughdrill, G.W.4    Lowry, D.F.5    Gomes, X.6    Wold, M.S.7
  • 21
    • 0033010511 scopus 로고    scopus 로고
    • Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 angstrom: Evidence for conformational lability
    • P. Holliger, L. Riechmann, and R.L. Williams Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 angstrom: evidence for conformational lability J. Mol. Biol. 288 1999 649 657
    • (1999) J. Mol. Biol. , vol.288 , pp. 649-657
    • Holliger, P.1    Riechmann, L.2    Williams, R.L.3
  • 22
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 angstrom resolution
    • R.B. Sutton, D. Fasshauer, R. Jahn, and A.T. Brunger Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 angstrom resolution Nature 395 1998 347 353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 23
    • 0001526540 scopus 로고
    • Phase-transitions in the 3-state antiferromagnetic potts-model
    • P.J. Kundrotas, S. Lapinskas, and A. Rosengren Phase-transitions in the 3-state antiferromagnetic potts-model Phys. Rev., B 52 1995 9166 9169
    • (1995) Phys. Rev., B , vol.52 , pp. 9166-9169
    • Kundrotas, P.J.1    Lapinskas, S.2    Rosengren, A.3
  • 24
    • 4243534976 scopus 로고
    • New numerical method to study phase-transitions
    • J.Y. Lee, and J.M. Kosterlitz New numerical method to study phase-transitions Phys. Rev. Lett. 65 1990 137 140
    • (1990) Phys. Rev. Lett. , vol.65 , pp. 137-140
    • Lee, J.Y.1    Kosterlitz, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.