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Volumn 60, Issue 4, 2005, Pages 679-689

Main-chain conformational tendencies of amino acids

Author keywords

Diversity space; Folding tendency; Ramachandran plot; Substitution table; Two dimensional map

Indexed keywords

AMINO ACID;

EID: 24644449168     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20530     Document Type: Article
Times cited : (139)

References (30)
  • 1
    • 73649194755 scopus 로고
    • Stereochemistry of polypeptide chain configurations
    • Ramachandran GN, Ramakrishnan C. Stereochemistry of polypeptide chain configurations. J Mol Biol 1963;7:95-99.
    • (1963) J Mol Biol , vol.7 , pp. 95-99
    • Ramachandran, G.N.1    Ramakrishnan, C.2
  • 2
    • 0037441479 scopus 로고    scopus 로고
    • Comparison of a QM/MM force field and molecular mechanics force fields in simulations of alanine and glycine "dipeptides" (Ace-Ala-Nme and Ace-Gly-Nme) in water in relation to the problem of modeling the unfolded peptide backbone in solution
    • Hu H, Elstner M, Hermans J. Comparison of a QM/MM force field and molecular mechanics force fields in simulations of alanine and glycine "dipeptides" (Ace-Ala-Nme and Ace-Gly-Nme) in water in relation to the problem of modeling the unfolded peptide backbone in solution. Proteins 2003;50:451-463.
    • (2003) Proteins , vol.50 , pp. 451-463
    • Hu, H.1    Elstner, M.2    Hermans, J.3
  • 3
    • 0142179047 scopus 로고    scopus 로고
    • Revisiting the Ramachandran plot: Hard-sphere repulsion, electrostatics, and H-bonding in the alpha-helix
    • Ho BK, Thomas A, Brasseur R. Revisiting the Ramachandran plot: hard-sphere repulsion, electrostatics, and H-bonding in the alpha-helix. Protein Sci 2003;12:2508-2522.
    • (2003) Protein Sci , vol.12 , pp. 2508-2522
    • Ho, B.K.1    Thomas, A.2    Brasseur, R.3
  • 4
  • 5
    • 0034994293 scopus 로고    scopus 로고
    • The interrelationships of side-chain and main-chain conformations in proteins
    • Chakrabarti P, Pal D. The interrelationships of side-chain and main-chain conformations in proteins. Prog Biophys Mol Biol 2001;76:1-102.
    • (2001) Prog Biophys Mol Biol , vol.76 , pp. 1-102
    • Chakrabarti, P.1    Pal, D.2
  • 6
  • 9
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph 1990;8:29,52-56.
    • (1990) J Mol Graph , vol.8 , pp. 29
    • Vriend, G.1
  • 11
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 12
    • 0033977581 scopus 로고    scopus 로고
    • The ASTRAL compendium for protein structure and sequence analysis
    • Brenner SE, Koehl P, Levitt M. The ASTRAL compendium for protein structure and sequence analysis. Nucleic Acids Res 2000;28:254-256.
    • (2000) Nucleic Acids Res , vol.28 , pp. 254-256
    • Brenner, S.E.1    Koehl, P.2    Levitt, M.3
  • 13
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt GJ, Jones TA. Phi/psi-chology: Ramachandran revisited. Structure 1996;4:1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 17
    • 0033584887 scopus 로고    scopus 로고
    • Cis peptide bonds in proteins: Residues involved, their conformations, interactions and locations
    • Pal D, Chakrabarti P. Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations. J Mol Biol 1999;294:271-288.
    • (1999) J Mol Biol , vol.294 , pp. 271-288
    • Pal, D.1    Chakrabarti, P.2
  • 18
    • 0030598361 scopus 로고    scopus 로고
    • Disallowed Ramachandran conformations of amino acid residues in protein structures
    • Gunasekaran K, Ramakrishnan C, Balaram P. Disallowed Ramachandran conformations of amino acid residues in protein structures. J Mol Biol 1996;264:191-198.
    • (1996) J Mol Biol , vol.264 , pp. 191-198
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 19
    • 0036173727 scopus 로고    scopus 로고
    • On residues in the disallowed region of the Ramachandran map
    • Pal D, Chakrabarti P. On residues in the disallowed region of the Ramachandran map. Biopolymers 2002;63:195-206.
    • (2002) Biopolymers , vol.63 , pp. 195-206
    • Pal, D.1    Chakrabarti, P.2
  • 20
    • 0023488772 scopus 로고
    • Which organic compounds could have occurred on the prebiotic earth?
    • Miller SL. Which organic compounds could have occurred on the prebiotic earth? Cold Spring Harb Symp Quant Biol 1987;52:17-27.
    • (1987) Cold Spring Harb Symp Quant Biol , vol.52 , pp. 17-27
    • Miller, S.L.1
  • 21
    • 0001150856 scopus 로고    scopus 로고
    • Glycine clock: Eubacteria first, archaea next, protoctista, fungi, planta and animalia at last
    • Trifonov EN. Glycine clock: eubacteria first, archaea next, protoctista, fungi, planta and animalia at last. Gene Ther Mol Biol 1999;4:313-323.
    • (1999) Gene Ther Mol Biol , vol.4 , pp. 313-323
    • Trifonov, E.N.1
  • 22
    • 0034736513 scopus 로고    scopus 로고
    • Consensus temporal order of amino acids and evolution of the triplet code
    • Trifonov EN. Consensus temporal order of amino acids and evolution of the triplet code. Gene 2000;261:139-151.
    • (2000) Gene , vol.261 , pp. 139-151
    • Trifonov, E.N.1
  • 23
    • 24644495972 scopus 로고    scopus 로고
    • Cunningham BC, Lowman HB, Wells JA et al, inventors. Genetech I, assignee. Human Growth Hormone Variants. USA patent WO 97/11178. Mar 1997
    • Cunningham BC, Lowman HB, Wells JA et al, inventors. Genetech I, assignee. Human Growth Hormone Variants. USA patent WO 97/11178. Mar 1997.
  • 25
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham BC, Wells JA. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 1989;244:1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 26
    • 24644431754 scopus 로고    scopus 로고
    • Filikov A, inventor. Xencor I, assignee. Novel nucleic acids and proteins with growth hormone activity. USA patent WO 00/68385. Nov 2000
    • Filikov A, inventor. Xencor I, assignee. Novel nucleic acids and proteins with growth hormone activity. USA patent WO 00/68385. Nov 2000.
  • 27
    • 0029147823 scopus 로고
    • Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures
    • Swindells MB, MacArthur MW, Thornton JM. Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures. Nat Struct Biol 1995;2:596-603.
    • (1995) Nat Struct Biol , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 28
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B, Kajava AV. The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 2001;11:725-732.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 29
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou PY, Fasman GD. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 1974;13:211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 30
    • 0036878154 scopus 로고    scopus 로고
    • An analysis of protein domain linkers: Their classification and role in protein folding
    • George RA, Heringa J. An analysis of protein domain linkers: their classification and role in protein folding. Protein Eng 2002;15:871-879.
    • (2002) Protein Eng , vol.15 , pp. 871-879
    • George, R.A.1    Heringa, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.