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Volumn 163-164, Issue , 2012, Pages 21-34

Experimentally assessing molecular dynamics sampling of the protein native state conformational distribution

Author keywords

Continuum electrostatics; Hydrogen exchange; Protein ensemble; Protein flexibility

Indexed keywords

APROTININ; LYSINE; PROTEASOME; UBIQUITIN;

EID: 84862817200     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2012.02.002     Document Type: Article
Times cited : (12)

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    • A highly destabilizing mutation, G37A, of the bovine pancreatic trypsin inhibitor retains the average native conformation but greatly increases local flexibility
    • DOI 10.1021/bi011693e
    • J.L. Battiste, R. Li, and C. Woodward A highly destabilizing mutation, G37A, of the bovine pancreatic trypsin inhibitor retains the average native conformation but greatly increases local flexibility Biochemistry 41 2002 2237 2245 (Pubitemid 34160884)
    • (2002) Biochemistry , vol.41 , Issue.7 , pp. 2237-2245
    • Battiste, J.L.1    Li, R.2    Woodward, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.