메뉴 건너뛰기




Volumn 37, Issue 1, 1999, Pages 44-55

Strain in protein structures as viewed through nonrotameric side chains: II. Effects upon ligand binding

Author keywords

Catalysis; Ligand binding; Product formation; Protein folding; Protein structure; Rotamers

Indexed keywords

AMINO ACID; APOPROTEIN; ASPARAGINE; ASPARTIC ACID; GLUTAMIC ACID; HISTIDINE; LIGAND; METHIONINE; PROTEIN;

EID: 0033215221     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991001)37:1<44::AID-PROT5>3.0.CO;2-F     Document Type: Article
Times cited : (33)

References (21)
  • 1
    • 0027208112 scopus 로고
    • Rotamers: To be or not to be? An analysis of amino acid side-chain conformations in globular proteins
    • Schrauber H, Eisenhaber F, Argos P. Rotamers: to be or not to be? An analysis of amino acid side-chain conformations in globular proteins. J Mol Biol 1993;230:592-612.
    • (1993) J Mol Biol , vol.230 , pp. 592-612
    • Schrauber, H.1    Eisenhaber, F.2    Argos, P.3
  • 2
    • 0018115846 scopus 로고
    • Conformations of amino acid side-chains in proteins
    • Janin J, Wodak S, Levitt M, Maigret B. Conformations of amino acid side-chains in proteins. J Mol Biol 1978;125:357-386, 1978.
    • (1978) J Mol Biol , vol.125 , pp. 357-386
    • Janin, J.1    Wodak, S.2    Levitt, M.3    Maigret, B.4
  • 4
    • 0000850121 scopus 로고
    • Side-chain torsional potentials and motion of amino acids in proteins: Bovine pancreatic trypsin inhibitor
    • Ghelin BR, Karplus M. Side-chain torsional potentials and motion of amino acids in proteins: bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci USA 1975;72:2002-2006.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2002-2006
    • Ghelin, B.R.1    Karplus, M.2
  • 5
    • 0018780591 scopus 로고
    • Side-chain torsional potentials: Effect of dipeptide, protein and solvent environment
    • Ghelin BR, Karplus M. Side-chain torsional potentials: effect of dipeptide, protein and solvent environment. Biochemistry 1979;18: 1256-1268.
    • (1979) Biochemistry , vol.18 , pp. 1256-1268
    • Ghelin, B.R.1    Karplus, M.2
  • 6
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder JW, Richards FM. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J Mol Biol 1987;193:775-791.
    • (1987) J Mol Biol , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 7
    • 0026665778 scopus 로고
    • Side-chain entropy opposes α-helix formation but rationalizes experimentally determined helix-forming propensities
    • Creamer TP, Rose GD. Side-chain entropy opposes α-helix formation but rationalizes experimentally determined helix-forming propensities. Proc Natl Acad Sci USA 1992;89:5937-5941.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5937-5941
    • Creamer, T.P.1    Rose, G.D.2
  • 8
    • 0027991081 scopus 로고
    • Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation
    • Lee KH, Xie D, Amzel LM. Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation. Proteins 1994;20:68-84.
    • (1994) Proteins , vol.20 , pp. 68-84
    • Lee, K.H.1    Xie, D.2    Amzel, L.M.3
  • 9
    • 0026055156 scopus 로고
    • Analysis of steric strain in the polypeptide backbone of protein molecules
    • Herzberg O, Moult J. Analysis of steric strain in the polypeptide backbone of protein molecules. Proteins 1991;11:223-229.
    • (1991) Proteins , vol.11 , pp. 223-229
    • Herzberg, O.1    Moult, J.2
  • 10
    • 0033213892 scopus 로고    scopus 로고
    • Strain in protein structures as viewed through non-rotameric side-chains. I. Spatial position and interaction
    • Heringa J, Argos P. Strain in protein structures as viewed through non-rotameric side-chains. I. Spatial position and interaction. Proteins 1999;37:30-43.
    • (1999) Proteins , vol.37 , pp. 30-43
    • Heringa, J.1    Argos, P.2
  • 12
    • 0027102226 scopus 로고
    • OBSTRUCT: A program to obtain largest cliques from a protein sequence set according to structural resolution and sequence similarity
    • Heringa J, Sommerfeldt H, Higgins D, Argos P. OBSTRUCT: a program to obtain largest cliques from a protein sequence set according to structural resolution and sequence similarity. Comput Appl Biosci 1992;8:599-600.
    • (1992) Comput Appl Biosci , vol.8 , pp. 599-600
    • Heringa, J.1    Sommerfeldt, H.2    Higgins, D.3    Argos, P.4
  • 13
    • 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
  • 14
    • 84986522918 scopus 로고
    • ICM - A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation
    • Abagyan R, Totrov M, Kuznetsov D. ICM - a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J Comp Chem 1994;15:488-506.
    • (1994) J Comp Chem , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.3
  • 15
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM. Satisfying hydrogen bonding potential in proteins. J Mol Biol 1994;238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 17
    • 0025789054 scopus 로고
    • Side-chain clusters in protein structures and their role in protein folding
    • Heringa J, Argos P. Side-chain clusters in protein structures and their role in protein folding. J Mol Biol 1991;220:151-171.
    • (1991) J Mol Biol , vol.220 , pp. 151-171
    • Heringa, J.1    Argos, P.2
  • 18
    • 0017881332 scopus 로고
    • The α-helix dipole and the properties of proteins
    • Hol WGJ, van Duijnen PT, Berendsen HJC. The α-helix dipole and the properties of proteins. Nature 1978;273:443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 19
    • 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
  • 20
    • 0024349252 scopus 로고
    • Protein structure alignment
    • Taylor WR, Orengo CA. Protein structure alignment. J Mol Biol 1989;208:1-22.
    • (1989) J Mol Biol , vol.208 , pp. 1-22
    • Taylor, W.R.1    Orengo, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.