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Volumn 6, Issue 7, 1999, Pages 672-682

A protein taxonomy based on secondary structure

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ANALYSIS;

EID: 0033056948     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/10728     Document Type: Article
Times cited : (103)

References (10)
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  • 2
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    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itahaki, L.S., Otzen, D.E. & Fersht, A.R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254, 260-288 (1995).
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    • Itahaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 3
    • 0032568498 scopus 로고    scopus 로고
    • Single-tryptophan mutants of monomeric tryptophan repressor: Optical spectroscopy reveals nonnative structure in a model for an early folding intermediate
    • Shao, X. & Matthews, C.R. Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Biochemistry 37, 7850-7858 (1998).
    • (1998) Biochemistry , vol.37 , pp. 7850-7858
    • Shao, X.1    Matthews, C.R.2
  • 4
    • 0030716169 scopus 로고    scopus 로고
    • Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein
    • Clark, P.L., Liu, Z.-P., Rizo, J. & Gierasch, L.M. Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein. Nature Struct. Biol. 4, 883-886 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 883-886
    • Clark, P.L.1    Liu, Z.-P.2    Rizo, J.3    Gierasch, L.M.4
  • 5
    • 0028124611 scopus 로고
    • Does compactness induce secondary structure in proteins? A study of poly-alanine chains computed by distance geometry
    • Yee, D.P., Chan, H.S., Havel, T.F. & Dill, K.A. Does compactness induce secondary structure in proteins? A study of poly-alanine chains computed by distance geometry. J. Mol. Biol. 241, 557-573 (1994).
    • (1994) J. Mol. Biol. , vol.241 , pp. 557-573
    • Yee, D.P.1    Chan, H.S.2    Havel, T.F.3    Dill, K.A.4
  • 6
    • 84985641098 scopus 로고
    • Effects of distance constraints on macromolecular conformation. II. Simulation of experimental results and theoretical predictions
    • Havel, T.F., Grippen, G.M. & Kuntz, I.D. Effects of distance constraints on macromolecular conformation. II. Simulation of experimental results and theoretical predictions. Biopolymers 18, 73-81 (1979).
    • (1979) Biopolymers , vol.18 , pp. 73-81
    • Havel, T.F.1    Grippen, G.M.2    Kuntz, I.D.3
  • 7
    • 0030947929 scopus 로고    scopus 로고
    • Folding propensities of peptide fragments of myoglobin
    • Reymond, M.T., Merutka, G., Dyson, H.J. & Wright, P.E. Folding propensities of peptide fragments of myoglobin. Protein Sci. 6, 706-716 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 706-716
    • Reymond, M.T.1    Merutka, G.2    Dyson, H.J.3    Wright, P.E.4
  • 8
    • 0026743136 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding II. Plastocyanin
    • Dyson, H.J. et al. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding II. Plastocyanin. J. Mol. Biol. 226, 819-835 (1992).
    • (1992) J. Mol. Biol. , vol.226 , pp. 819-835
    • Dyson, H.J.1
  • 9
    • 0029055313 scopus 로고
    • LINUS - A simple algorithm to predict the fold of a protein
    • Srinivasan, R. & Rose, G.D. LINUS - a simple algorithm to predict the fold of a protein. Proteins Struct. Funct. Genet 22, 81-99 (1995).
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.