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Volumn 63, Issue 2, 2006, Pages 356-372

Mutations in α-helical solvent-exposed sites of eglin c have long-range effects: Evidence from molecular dynamics simulations

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; EGLIN C; GLUTAMIC ACID; PROTEINASE INHIBITOR;

EID: 33645281415     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20794     Document Type: Article
Times cited : (8)

References (60)
  • 1
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil KT, DeGrado WF. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 1990;250:646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 2
    • 0026058806 scopus 로고
    • Physical reasons for secondary structure stability: Alpha-helices in short peptides
    • Finkelstein AV, Badretdinov AY, Ptitsyn OB. Physical reasons for secondary structure stability: alpha-helices in short peptides. Proteins 1991;10:287-299.
    • (1991) Proteins , vol.10 , pp. 287-299
    • Finkelstein, A.V.1    Badretdinov, A.Y.2    Ptitsyn, O.B.3
  • 3
    • 0027236794 scopus 로고
    • Structural basis of amino acid alpha helix propensity
    • Blaber M, Zhang XJ, Matthews BW. Structural basis of amino acid alpha helix propensity. Science 1993;260:1637-1640.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.J.2    Matthews, B.W.3
  • 4
    • 0029958659 scopus 로고    scopus 로고
    • Structure-based thermodynamic scale of alpha-helix propensities in amino acids
    • Luque I, Mayorga OL, Freire E. Structure-based thermodynamic scale of alpha-helix propensities in amino acids. Biochemistry 1996;35:13681-13688.
    • (1996) Biochemistry , vol.35 , pp. 13681-13688
    • Luque, I.1    Mayorga, O.L.2    Freire, E.3
  • 5
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Munoz V, Serrano L. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 1997;41:495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 6
    • 0017881332 scopus 로고
    • The alpha-helix dipole and the properties of proteins
    • Hol WG, van Duijnen PT, Berendsen HJ. The alpha-helix dipole and the properties of proteins. Nature 1978;273:443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.1    Van Duijnen, P.T.2    Berendsen, H.J.3
  • 7
    • 0025260032 scopus 로고
    • Side chain contributions to the stability of alpha-helical structure in peptides
    • Lyu PC, Liff MI, Marky LA, Kallenbach NR. Side chain contributions to the stability of alpha-helical structure in peptides. Science 1990;250:669-673.
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 8
    • 0026709329 scopus 로고
    • Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces
    • Serrano L, Sancho J, Hirshberg M, Fersht AR. Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. J Mol Biol 1992;227:544-559.
    • (1992) J Mol Biol , vol.227 , pp. 544-559
    • Serrano, L.1    Sancho, J.2    Hirshberg, M.3    Fersht, A.R.4
  • 9
    • 0017292056 scopus 로고
    • The alpha-helix as an electric macro-dipole
    • Wada A. The alpha-helix as an electric macro-dipole. Adv Biophys 1976:1-63.
    • (1976) Adv Biophys , pp. 1-63
    • Wada, A.1
  • 10
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta LG, Rose GD. Helix signals in proteins. Science 1988;240:1632-1641.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 11
    • 0027204024 scopus 로고
    • Helix stop signals in proteins and peptides: The capping box
    • Harper ET, Rose GD. Helix stop signals in proteins and peptides: the capping box. Biochemistry 1993;32:7605-7609.
    • (1993) Biochemistry , vol.32 , pp. 7605-7609
    • Harper, E.T.1    Rose, G.D.2
  • 12
    • 0029020484 scopus 로고
    • N- and C-capping preferences for all 20 amino acids in alpha-helical peptides
    • Doig AJ, Baldwin RL. N- and C-capping preferences for all 20 amino acids in alpha-helical peptides. Protein Sci 1995;4:1325-1336.
    • (1995) Protein Sci , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 13
    • 0028173780 scopus 로고
    • Rules for a-helix termination by glycine
    • Aurora R, Srinivasan R, Rose GD. Rules for a-helix termination by glycine. Science 1994;264:1126-1130.
    • (1994) Science , vol.264 , pp. 1126-1130
    • Aurora, R.1    Srinivasan, R.2    Rose, G.D.3
  • 14
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α helices
    • Richardson JS, Richardson DC. Amino acid preferences for specific locations at the ends of α helices. Science 1988;240:1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 15
    • 0038275884 scopus 로고    scopus 로고
    • Testing hypotheses about determinants of protein structure with high-precision, high-throughput stability measurements and statistical modeling
    • Yi F, Sims DA, Pielak GJ, Edgell MH. Testing hypotheses about determinants of protein structure with high-precision, high-throughput stability measurements and statistical modeling. Biochemistry 2003;42:7594-7603.
    • (2003) Biochemistry , vol.42 , pp. 7594-7603
    • Yi, F.1    Sims, D.A.2    Pielak, G.J.3    Edgell, M.H.4
  • 16
    • 0037295565 scopus 로고    scopus 로고
    • Dynamic effects of mutations within two loops of cytochrome c551 from Pseudomonas aeruginosa
    • Ceruso MA, Grottesi A, Di Nola A. Dynamic effects of mutations within two loops of cytochrome c551 from Pseudomonas aeruginosa. Proteins 2003;50:222-229.
    • (2003) Proteins , vol.50 , pp. 222-229
    • Ceruso, M.A.1    Grottesi, A.2    Di Nola, A.3
  • 17
    • 0038810233 scopus 로고    scopus 로고
    • Correlated motion and the effect of distal mutations in dihydrofolate reductase
    • Rod TH, Radkiewicz JL, Brooks 3rd CL. Correlated motion and the effect of distal mutations in dihydrofolate reductase. Proc Natl Acad Sci USA 2003;100:6980-6985.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6980-6985
    • Rod, T.H.1    Radkiewicz, J.L.2    Brooks III, C.L.3
  • 18
    • 0032529585 scopus 로고    scopus 로고
    • Dynamic structure of subtilisin-eglin c complex studied by normal mode analysis
    • Ishida H, Jochi Y, Kidera A. Dynamic structure of subtilisin-eglin c complex studied by normal mode analysis. Proteins 1998;32:324-333.
    • (1998) Proteins , vol.32 , pp. 324-333
    • Ishida, H.1    Jochi, Y.2    Kidera, A.3
  • 19
    • 4744347909 scopus 로고    scopus 로고
    • Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c
    • Clarkson MW, Lee AL. Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c. Biochemistry 2004;43:12448-12458.
    • (2004) Biochemistry , vol.43 , pp. 12448-12458
    • Clarkson, M.W.1    Lee, A.L.2
  • 20
    • 0027339381 scopus 로고
    • 13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin inhibitor 2: Correlations with structure and stability
    • Matthews SJ, Jandu SK, Leatherbarrow RJ. 13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin inhibitor 2: correlations with structure and stability. Biochemistry 1993;32:657-662.
    • (1993) Biochemistry , vol.32 , pp. 657-662
    • Matthews, S.J.1    Jandu, S.K.2    Leatherbarrow, R.J.3
  • 21
    • 0019270387 scopus 로고
    • Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis
    • Seemuller U, Eulitz M, Fritz H, Strobl A. Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis. Hoppe Seylers Z Physiol Chem 1980;361:1841-1846.
    • (1980) Hoppe Seylers Z Physiol Chem , vol.361 , pp. 1841-1846
    • Seemuller, U.1    Eulitz, M.2    Fritz, H.3    Strobl, A.4
  • 22
    • 17744395510 scopus 로고    scopus 로고
    • Sensitivity of the folding/unfolding transition state ensemble of chymotrypsin inhibitor 2 to changes in temperature and solvent
    • Day R, Daggett V. Sensitivity of the folding/unfolding transition state ensemble of chymotrypsin inhibitor 2 to changes in temperature and solvent. Protein Sci 2005;14:1242-1252.
    • (2005) Protein Sci , vol.14 , pp. 1242-1252
    • Day, R.1    Daggett, V.2
  • 23
    • 2342614722 scopus 로고    scopus 로고
    • Counteraction of urea-induced protein denaturation by trimethylamine N-oxide: A chemical chaperone at atomic resolution
    • Bennion BJ, Daggett V. Counteraction of urea-induced protein denaturation by trimethylamine N-oxide: a chemical chaperone at atomic resolution. Proc Natl Acad Sci USA 2004;101:6433-6438.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6433-6438
    • Bennion, B.J.1    Daggett, V.2
  • 24
    • 0142153202 scopus 로고    scopus 로고
    • Structure-oriented rational design of chymotrypsin inhibitor models
    • Mucsi Z, Gaspari Z, Orosz G, Perczel A. Structure-oriented rational design of chymotrypsin inhibitor models. Protein Eng 2003;16:673-681.
    • (2003) Protein Eng , vol.16 , pp. 673-681
    • Mucsi, Z.1    Gaspari, Z.2    Orosz, G.3    Perczel, A.4
  • 25
    • 0035223268 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein unfolding/folding
    • Daggett V. Molecular dynamics simulations of protein unfolding/folding. Methods Mol Biol 2001;168:215-247.
    • (2001) Methods Mol Biol , vol.168 , pp. 215-247
    • Daggett, V.1
  • 26
    • 0035029408 scopus 로고    scopus 로고
    • Conformational dynamics of subtilisin-chymotrypsin inhibitor 2 complex by coarse-grained simulations
    • Kurt N, Haliloglu T. Conformational dynamics of subtilisin-chymotrypsin inhibitor 2 complex by coarse-grained simulations. J Biomol Struct Dyn 2001;18:713-731.
    • (2001) J Biomol Struct Dyn , vol.18 , pp. 713-731
    • Kurt, N.1    Haliloglu, T.2
  • 27
    • 0345281586 scopus 로고    scopus 로고
    • Conformational dynamics of chymotrypsin inhibitor 2 by coarse-grained simulations
    • Kurt N, Haliloglu T. Conformational dynamics of chymotrypsin inhibitor 2 by coarse-grained simulations. Proteins 1999;37:454-464.
    • (1999) Proteins , vol.37 , pp. 454-464
    • Kurt, N.1    Haliloglu, T.2
  • 28
    • 0029586380 scopus 로고
    • Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: Comparison to x-ray crystallographic and NMR data
    • Li A, Daggett V. Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: comparison to x-ray crystallographic and NMR data. Protein Eng 1995;8:1117-1128.
    • (1995) Protein Eng , vol.8 , pp. 1117-1128
    • Li, A.1    Daggett, V.2
  • 30
    • 0031552590 scopus 로고    scopus 로고
    • Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature
    • Itzhaki LS, Neira JL, Fersht AR. Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature. J Mol Biol 1997;270:89-98.
    • (1997) J Mol Biol , vol.270 , pp. 89-98
    • Itzhaki, L.S.1    Neira, J.L.2    Fersht, A.R.3
  • 31
    • 0031296703 scopus 로고    scopus 로고
    • Strain in the folding nucleus of chymotrypsin inhibitor 2
    • Ladurner AG, Itzhaki LS, Fersht AR. Strain in the folding nucleus of chymotrypsin inhibitor 2. Fold Des 1997;2:363-368.
    • (1997) Fold des , vol.2 , pp. 363-368
    • Ladurner, A.G.1    Itzhaki, L.S.2    Fersht, A.R.3
  • 33
    • 0027092679 scopus 로고
    • The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures
    • Hyberts SG, Goldberg MS, Havel TF, Wagner G. The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures. Protein Sci 1992;1:736-751.
    • (1992) Protein Sci , vol.1 , pp. 736-751
    • Hyberts, S.G.1    Goldberg, M.S.2    Havel, T.F.3    Wagner, G.4
  • 35
    • 0023643147 scopus 로고
    • The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry
    • Bode W, Papamokos E, Musil D. The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry. Eur J Biochem 1987;166:673-692.
    • (1987) Eur J Biochem , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 37
    • 0008524099 scopus 로고
    • Crystallographic refinement by incorporation of molecular dynamics: Thermostable serine protease thermitase complexed with eglin c
    • Gros P, Fujinaga M, Dijkstra BW, Kalk KH, Hol WG. Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c. Acta Crystallogr B Biol Crystallogr 1989;45:488-499.
    • (1989) Acta Crystallogr B Biol Crystallogr , vol.45 , pp. 488-499
    • Gros, P.1    Fujinaga, M.2    Dijkstra, B.W.3    Kalk, K.H.4    Hol, W.G.5
  • 38
    • 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
  • 39
    • 0029981188 scopus 로고    scopus 로고
    • Structure of the transition state for folding of a protein derived from experiment and simulation
    • Daggett V, Li A, Itzhaki LS, Otzen DE, Fersht AR. Structure of the transition state for folding of a protein derived from experiment and simulation. J Mol Biol 1996;257:430-440.
    • (1996) J Mol Biol , vol.257 , pp. 430-440
    • Daggett, V.1    Li, A.2    Itzhaki, L.S.3    Otzen, D.E.4    Fersht, A.R.5
  • 40
    • 0029963345 scopus 로고    scopus 로고
    • Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations
    • Li A, Daggett V. Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations. J Mol Biol 1996;257:412-429.
    • (1996) J Mol Biol , vol.257 , pp. 412-429
    • Li, A.1    Daggett, V.2
  • 41
    • 0036968512 scopus 로고    scopus 로고
    • Increasing temperature accelerates protein unfolding without changing the pathway of unfolding
    • Day R, Bennion BJ, Ham S, Daggett V. Increasing temperature accelerates protein unfolding without changing the pathway of unfolding. J Mol Biol 2002;322:189-203.
    • (2002) J Mol Biol , vol.322 , pp. 189-203
    • Day, R.1    Bennion, B.J.2    Ham, S.3    Daggett, V.4
  • 42
    • 0036306054 scopus 로고    scopus 로고
    • Probing the energy landscape of protein folding/unfolding transition states
    • De Jong D, Riley R, Alonso DO, Daggett V. Probing the energy landscape of protein folding/unfolding transition states. J Mol Biol 2002;319:229-242.
    • (2002) J Mol Biol , vol.319 , pp. 229-242
    • De Jong, D.1    Riley, R.2    Alonso, D.O.3    Daggett, V.4
  • 43
    • 0035836687 scopus 로고    scopus 로고
    • Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution
    • Kazmirski SL, Wong KB, Freund SM, Tan YJ, Fersht AR, Daggett V. Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution. Proc Natl Acad Sci USA 2001;98:4349-4354.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4349-4354
    • Kazmirski, S.L.1    Wong, K.B.2    Freund, S.M.3    Tan, Y.J.4    Fersht, A.R.5    Daggett, V.6
  • 44
    • 0034657550 scopus 로고    scopus 로고
    • Computer simulations of protein folding by targeted molecular dynamics
    • Ferrara P, Apostolakis J, Caflisch A. Computer simulations of protein folding by targeted molecular dynamics. Proteins 2000;39:252-260.
    • (2000) Proteins , vol.39 , pp. 252-260
    • Ferrara, P.1    Apostolakis, J.2    Caflisch, A.3
  • 45
    • 0032555115 scopus 로고    scopus 로고
    • Synergy between simulation and experiment in describing the energy landscape of protein folding
    • Ladurner AG, Itzhaki LS, Daggett V, Fersht AR. Synergy between simulation and experiment in describing the energy landscape of protein folding. Proc Natl Acad Sci USA 1998;95:8473-8478.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8473-8478
    • Ladurner, A.G.1    Itzhaki, L.S.2    Daggett, V.3    Fersht, A.R.4
  • 46
    • 0035814880 scopus 로고    scopus 로고
    • Direct comparison of experimental and calculated folding free energies for hydrophobic deletion mutants of chymotrypsin inhibitor 2: Free energy perturbation calculations using transition and denatured states from molecular dynamics simulations of unfolding
    • Pan Y, Daggett V. Direct comparison of experimental and calculated folding free energies for hydrophobic deletion mutants of chymotrypsin inhibitor 2: free energy perturbation calculations using transition and denatured states from molecular dynamics simulations of unfolding. Biochemistry 2001;40:2723-2731.
    • (2001) Biochemistry , vol.40 , pp. 2723-2731
    • Pan, Y.1    Daggett, V.2
  • 47
    • 0345707599 scopus 로고    scopus 로고
    • Increased rigidity of eglin c at acidic pH: Evidence from NMR spin relaxation and MD simulations
    • Hu H, Clarkson MW, Hermans J, Lee AL. Increased rigidity of eglin c at acidic pH: evidence from NMR spin relaxation and MD simulations. Biochemistry 2003;42:13856-13868.
    • (2003) Biochemistry , vol.42 , pp. 13856-13868
    • Hu, H.1    Clarkson, M.W.2    Hermans, J.3    Lee, A.L.4
  • 50
    • 0000224283 scopus 로고    scopus 로고
    • CHARMM: The energy function and its parameterization with an overview of the program
    • Schleyer PvR, Schreiner PR, Allinger NL, Clark T, Gasteiger J, Kollman P, III HFS, editors. Chichester: Wiley
    • MacKerell Jr. AD, Brooks B, Brooks III CL, Nilsson L, Roux B, Won Y, Karplus M. CHARMM: the energy function and its parameterization with an overview of the program. In: Schleyer PvR, Schreiner PR, Allinger NL, Clark T, Gasteiger J, Kollman P, III HFS, editors. The encyclopedia of computational chemistry, Volume 1. Chichester: Wiley; 1998. p 271-277.
    • (1998) The Encyclopedia of Computational Chemistry , vol.1 , pp. 271-277
    • MacKerell Jr., A.D.1    Brooks, B.2    Brooks III, C.L.3    Nilsson, L.4    Roux, B.5    Won, Y.6    Karplus, M.7
  • 51
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 1977;23:327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 53
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye T, Karplus M. Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins 1991;11:205-217.
    • (1991) Proteins , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 54
    • 0033955055 scopus 로고    scopus 로고
    • I. Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase
    • Radkiewicz JL, Brooks CL. I. Protein dynamics in enzymatic catalysis: exploration of dihydrofolate reductase. J Am Chem Soc 2000;122:225-231.
    • (2000) J Am Chem Soc , vol.122 , pp. 225-231
    • Radkiewicz, J.L.1    Brooks, C.L.2
  • 55
    • 0029623152 scopus 로고
    • Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields
    • Peng JW, Wagner G. Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields. Biochemistry 1995;34:16733-16752.
    • (1995) Biochemistry , vol.34 , pp. 16733-16752
    • Peng, J.W.1    Wagner, G.2
  • 56
    • 0033988897 scopus 로고    scopus 로고
    • Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex
    • Lee AL, Kinnear SA, Wand AJ. Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Nat Struct Biol 2000;7:72-77.
    • (2000) Nat Struct Biol , vol.7 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 57
    • 0035901519 scopus 로고    scopus 로고
    • An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs
    • Loh AP, Pawley N, Nicholson LK, Oswald RE. An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs. Biochemistry 2001;40:4590-4600.
    • (2001) Biochemistry , vol.40 , pp. 4590-4600
    • Loh, A.P.1    Pawley, N.2    Nicholson, L.K.3    Oswald, R.E.4
  • 58
    • 0036385729 scopus 로고    scopus 로고
    • Side-chain dynamics of the SAP SH2 domain correlate with a binding hot spot and a region with conformational plasticity
    • Finerty Jr. PJ. Muhandiram R, Forman-Kay JD. Side-chain dynamics of the SAP SH2 domain correlate with a binding hot spot and a region with conformational plasticity. J Mol Biol 2002;322:605-620.
    • (2002) J Mol Biol , vol.322 , pp. 605-620
    • Finerty Jr., P.J.1    Muhandiram, R.2    Forman-Kay, J.D.3
  • 59
    • 0347753736 scopus 로고    scopus 로고
    • Ligand-dependent dynamics and intramolecular signaling in a PDZ domain
    • Fuentes EJ, Der CJ, Lee AL. Ligand-dependent dynamics and intramolecular signaling in a PDZ domain. J Mol Biol 2004;335:1105-1115.
    • (2004) J Mol Biol , vol.335 , pp. 1105-1115
    • Fuentes, E.J.1    Der, C.J.2    Lee, A.L.3


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