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Volumn 303, Issue 2, 2000, Pages 125-130

Increasing the thermostability of staphylococcal nuclease: Implications for the origin of protein thermostability

Author keywords

Hydrogen bonding; Packing; Stabilization; Van der Waals interactions

Indexed keywords

NUCLEASE;

EID: 0034692902     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4140     Document Type: Article
Times cited : (118)

References (29)
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    • 0026755510 scopus 로고
    • Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: Evidence for mutational effects on the free energy of the denatured state
    • (1992) Biochemistry , vol.31 , pp. 5717-5728
    • Green, S.M.1    Meeker, A.K.2    Shortle, D.3
  • 6
    • 0003682904 scopus 로고
    • The role of interior side-chain packing in protein folding stability
    • The Protein Folding Problem and Tertiary Structure Prediction (Merz, K. M., Jr and Le Grand, S. M., eds), Birkhauser, Boston
    • (1994) , pp. 549-578
    • Hurley, J.H.1
  • 11
  • 20
    • 0022571680 scopus 로고
    • Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease
    • (1986) J. Cell Biochem. , vol.30 , pp. 281-289
    • Shortle, D.1
  • 23
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • (2000) Struct. Fold. Des. , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.