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Volumn 47, Issue 2, 2002, Pages 154-162

Role of hydrophilic and hydrophobic contacts in folding of the second β-hairpin fragment of protein G: Molecular dynamics simulation studies of an all-atom model

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN G;

EID: 0036568318     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10065     Document Type: Article
Times cited : (47)

References (44)
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    • Zhou, Y.1    Karplus, M.2
  • 40
    • 0028787226 scopus 로고
    • Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy
    • (1995) Protein Sci , vol.4 , pp. 2605-2615
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    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
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  • 43
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    • Understanding β-hairpin formation by molecular dynamics simulations of unfolding
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.