메뉴 건너뛰기




Volumn 60, Issue 4, 2005, Pages 732-739

Statistical characterization of salt bridges in proteins

Author keywords

Proteins structure and folding mechanism; Salt bridges

Indexed keywords

SOLVENT;

EID: 24644431966     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20549     Document Type: Article
Times cited : (58)

References (35)
  • 1
    • 0028177303 scopus 로고
    • DNA recognition by beta-sheets in the Arc repressor-operator crystal-structure
    • Raumann BE, Rould MA, Pabo CO, Sauer RT. DNA recognition by beta-sheets in the Arc repressor-operator crystal-structure. Nature 1994;367:754-757.
    • (1994) Nature , vol.367 , pp. 754-757
    • Raumann, B.E.1    Rould, M.A.2    Pabo, C.O.3    Sauer, R.T.4
  • 2
    • 0242407175 scopus 로고    scopus 로고
    • Structural determinants of SecB recognition by SecA in bacterial protein translocation
    • Zhou JH, Xu ZH. Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nat Struct Biol 2003;10:942-947.
    • (2003) Nat Struct Biol , vol.10 , pp. 942-947
    • Zhou, J.H.1    Xu, Z.H.2
  • 3
    • 0042347710 scopus 로고    scopus 로고
    • Surface salt bridges modulate DNA wrapping by the type II DNA-binding protein TF1
    • Grove A. Surface salt bridges modulate DNA wrapping by the type II DNA-binding protein TF1. Biochemistry 2003;42:8739-8747.
    • (2003) Biochemistry , vol.42 , pp. 8739-8747
    • Grove, A.1
  • 4
    • 0038650855 scopus 로고    scopus 로고
    • Comparison of calculation and experiment implicates significant electrostatic contributions to the binding stability of barnase and barstar
    • Dong F, Vijayakumar M, Zhou HX. Comparison of calculation and experiment implicates significant electrostatic contributions to the binding stability of barnase and barstar. Biophys J 2003;85:49-60.
    • (2003) Biophys J , vol.85 , pp. 49-60
    • Dong, F.1    Vijayakumar, M.2    Zhou, H.X.3
  • 5
    • 0042433116 scopus 로고    scopus 로고
    • New understandings of thermostable and peizostable enzymes
    • Yano JK, Poulos TL. New understandings of thermostable and peizostable enzymes. Curr Opin Biotechnol 2003;14:360-365.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 360-365
    • Yano, J.K.1    Poulos, T.L.2
  • 6
    • 0038339376 scopus 로고    scopus 로고
    • Allosteric communication in the tryptophan synthase bienzyme complex: Roles of the beta-subunit aspartate 305 arginine 141 salt bridge
    • Ferrari D, Niks D, Yang LH, Miles EW, Dunn MF. Allosteric communication in the tryptophan synthase bienzyme complex: roles of the beta-subunit aspartate 305 arginine 141 salt bridge. Biochemistry 2003;42:7807-7818.
    • (2003) Biochemistry , vol.42 , pp. 7807-7818
    • Ferrari, D.1    Niks, D.2    Yang, L.H.3    Miles, E.W.4    Dunn, M.F.5
  • 7
    • 0038047060 scopus 로고    scopus 로고
    • Electrostatic interactions in leucine zippers: Thermodynamic analysis of the contributions of Glu and his residues and the effect of mutating salt bridges
    • Marti DN, Bosshard HR. Electrostatic interactions in leucine zippers: thermodynamic analysis of the contributions of Glu and his residues and the effect of mutating salt bridges. J Mol Biol 2003;330:621-637.
    • (2003) J Mol Biol , vol.330 , pp. 621-637
    • Marti, D.N.1    Bosshard, H.R.2
  • 8
    • 0037864443 scopus 로고    scopus 로고
    • Design and application of basic amino acids displaying enhanced hydrophobicity
    • Kretsinger JK, Schneider JP. Design and application of basic amino acids displaying enhanced hydrophobicity. J Am Chem Soc 2003;125:7907-7913.
    • (2003) J Am Chem Soc , vol.125 , pp. 7907-7913
    • Kretsinger, J.K.1    Schneider, J.P.2
  • 9
    • 0027231258 scopus 로고
    • On the Ph-dependence of protein stability
    • Yang AS, Honig B. On the Ph-dependence of protein stability. J Mol Biol 1993;231:459-474.
    • (1993) J Mol Biol , vol.231 , pp. 459-474
    • Yang, A.S.1    Honig, B.2
  • 10
    • 0025718955 scopus 로고
    • Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis
    • Daopin S, Sauer U, Nicholson H, Matthews BW. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry 1991;30:7142-7153.
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Daopin, S.1    Sauer, U.2    Nicholson, H.3    Matthews, B.W.4
  • 11
    • 0028204490 scopus 로고
    • Do Salt bridges stabilize proteins - A continuum electrostatic analysis
    • Hendsch ZS, Tidor B. Do Salt bridges stabilize proteins-a continuum electrostatic analysis. Protein Sci 1994;3:211-226.
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 12
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger CD, Jonsson T, Sauer RT. Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. Proc Natl Acad Sci USA 1996;93:2629-2634.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 13
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity
    • Waldburger CD, Schildbach JF, Sauer RT. Are buried salt bridges important for protein stability and conformational specificity. Nat Struct Biol 1995;2:122-128.
    • (1995) Nat Struct Biol , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 14
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. Dominant forces in protein folding. Biochemistry 1990;29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 15
    • 0025663105 scopus 로고
    • Strength and cooperativity of contributions of surface salt bridges to protein stability
    • Horovitz A, Serrano L, Avron B, Bycroft M, Fersht AR. Strength and cooperativity of contributions of surface salt bridges to protein stability. J Mol Biol 1990;216:1031-1044.
    • (1990) J Mol Biol , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 16
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
    • Serrano L, Horovitz A, Avron B, Bycroft M, Fersht AR. Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. Biochemistry 1990;29:9343-9352.
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 17
    • 0028052741 scopus 로고
    • Contribution of a proline residue and a salt bridge to the stability of a type-I reverse turn in chymotrypsin inhibitor-2
    • Gay GD, Johnson CM, Fersht AR. Contribution of a proline residue and a salt bridge to the stability of a type-I reverse turn in chymotrypsin inhibitor-2. Protein Eng 1994;7:103-108.
    • (1994) Protein Eng , vol.7 , pp. 103-108
    • Gay, G.D.1    Johnson, C.M.2    Fersht, A.R.3
  • 18
    • 0028574137 scopus 로고
    • Contributions of a hydrogen-bond salt bridge network to the stability of secondary and tertiary structure in lambda-repressor
    • Marqusee S, Sauer RT. Contributions of a hydrogen-bond salt bridge network to the stability of secondary and tertiary structure in lambda-repressor. Protein Sci 1994;3:2217-2225.
    • (1994) Protein Sci , vol.3 , pp. 2217-2225
    • Marqusee, S.1    Sauer, R.T.2
  • 19
    • 0030596082 scopus 로고    scopus 로고
    • Structural role of a buried salt bridge in the 434 repressor DNA-binding domain
    • Pervushin K, Billeter M, Siegal G, Wuthrich K. Structural role of a buried salt bridge in the 434 repressor DNA-binding domain. J Mol Biol 1996;264:1002-1012.
    • (1996) J Mol Biol , vol.264 , pp. 1002-1012
    • Pervushin, K.1    Billeter, M.2    Siegal, G.3    Wuthrich, K.4
  • 20
    • 0030917740 scopus 로고    scopus 로고
    • Exceptionally stable salt bridges in cytochrome P450cam have functional roles
    • Lounnas V, Wade RC. Exceptionally stable salt bridges in cytochrome P450cam have functional roles. Biochemistry 1997;36:5402-5417.
    • (1997) Biochemistry , vol.36 , pp. 5402-5417
    • Lounnas, V.1    Wade, R.C.2
  • 22
    • 2942669906 scopus 로고    scopus 로고
    • Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding
    • Risal D, Gourinath S, Himmel DM, Szent-Gyorgyi AG, Cohen C. Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding. Proc Natl Acad Sci USA 2004;101:8930-8935.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8930-8935
    • Risal, D.1    Gourinath, S.2    Himmel, D.M.3    Szent-Gyorgyi, A.G.4    Cohen, C.5
  • 23
    • 0029986003 scopus 로고    scopus 로고
    • Patterns in ionizable side chain interactions in protein structures
    • Gandini D, Gogioso L, Bolognesi M, Bordo D. Patterns in ionizable side chain interactions in protein structures. Proteins 1996;24:439-449.
    • (1996) Proteins , vol.24 , pp. 439-449
    • Gandini, D.1    Gogioso, L.2    Bolognesi, M.3    Bordo, D.4
  • 24
    • 0033550299 scopus 로고    scopus 로고
    • Salt bridge stability in monomeric proteins
    • Kumar S, Nussinov R. Salt bridge stability in monomeric proteins. J Mol Biol 1999;293:1241-1255.
    • (1999) J Mol Biol , vol.293 , pp. 1241-1255
    • Kumar, S.1    Nussinov, R.2
  • 25
    • 0035327168 scopus 로고    scopus 로고
    • Protein flexibility and electrostatic interactions
    • Kumar S, Wolfson HJ, Nussinov R. Protein flexibility and electrostatic interactions. IBM J Res Dev 2001;45:499-512.
    • (2001) IBM J Res Dev , vol.45 , pp. 499-512
    • Kumar, S.1    Wolfson, H.J.2    Nussinov, R.3
  • 26
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • Kumar S, Nussinov R. Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys J 2002;83:1595-1612.
    • (2002) Biophys J , vol.83 , pp. 1595-1612
    • Kumar, S.1    Nussinov, R.2
  • 27
    • 0029588555 scopus 로고
    • Complex salt bridges in proteins-statistical-analysis of structure and function
    • Musafia B, Buchner V, Arad D. Complex salt bridges in proteins-statistical-analysis of structure and function. J Mol Biol 1995;254:761-770.
    • (1995) J Mol Biol , vol.254 , pp. 761-770
    • Musafia, B.1    Buchner, V.2    Arad, D.3
  • 29
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • Wang G, Dunbrack RLJ. PISCES: a protein sequence culling server. Bioinformatics 2003;19:1589-1591.
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack, R.L.J.2
  • 30
    • 0015222647 scopus 로고
    • Interpretation of protein structures-estimation of static accessibility
    • Lee B, Richards FM. Interpretation of protein structures-estimation of static accessibility. J Mol Biol 1971;55:379.
    • (1971) J Mol Biol , vol.55 , pp. 379
    • Lee, B.1    Richards, F.M.2
  • 32
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 34
    • 0033994586 scopus 로고    scopus 로고
    • Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers
    • Kumar S, Ma BY, Tsai CJ, Nussinov R. Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers. Proteins 2000;38:368-383.
    • (2000) Proteins , vol.38 , pp. 368-383
    • Kumar, S.1    Ma, B.Y.2    Tsai, C.J.3    Nussinov, R.4
  • 35
    • 0033104768 scopus 로고    scopus 로고
    • Hydrogen bonds between short polar side chains and peptide backbone: Prevalence in proteins and effects on helix-forming propensities
    • Vijayakumar M, Qian H, Zhou HX. Hydrogen bonds between short polar side chains and peptide backbone: prevalence in proteins and effects on helix-forming propensities. Proteins 1999;34:497-507.
    • (1999) Proteins , vol.34 , pp. 497-507
    • Vijayakumar, M.1    Qian, H.2    Zhou, H.X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.