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Volumn 409, Issue 6820, 2001, Pages 641-645

Three key residues form a critical contact network in a protein folding transition state

Author keywords

[No Author keywords available]

Indexed keywords

ACYLPHOSPHATASE;

EID: 0035252350     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35054591     Document Type: Article
Times cited : (404)

References (30)
  • 3
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    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1005-1009
    • Chiti, F.1
  • 7
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    • Protein structure determination in solution by nuclear magnetic resonance spectroscopy
    • (1989) Science , vol.243 , pp. 45-50
    • Wüthrich, K.1
  • 9
  • 10
    • 0034647415 scopus 로고    scopus 로고
    • Stabilisation of α-helices by site-directed mutagenesis reveals the secondary structure in the transition state for acylphosphatase folding
    • (2000) J. Mol. biol. , vol.300 , pp. 633-647
    • Taddei, N.1
  • 14
    • 0031465967 scopus 로고    scopus 로고
    • "New View" of protein folding reconciled with the old through multiple unfolding simulations
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 15
    • 0029151245 scopus 로고
    • First-principles calculation of the folding free energy of a three-helix bundle protein
    • (1995) Science , vol.269 , pp. 393-396
    • Boczko, E.M.1    Brooks, C.L.2
  • 30
    • 0000269043 scopus 로고    scopus 로고
    • Superparamagnetic clustering of data. The definitive solution of an ill posed problem
    • (1999) Physica A , vol.263 , pp. 158-169
    • Domany, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.