메뉴 건너뛰기




Volumn 268, Issue 12, 2001, Pages 3612-3618

Differentiation between conformational and autoproteolytic stability of the neutral protease from Bacillus stearothermophilus containing an engineered disulfide bond

Author keywords

Autoproteolysis; Disulfide bond; Neutral protease; Stability; Unfolding

Indexed keywords

DISULFIDE; GUANIDINE; NEUTRAL PROTEINASE;

EID: 0034819685     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02270.x     Document Type: Article
Times cited : (26)

References (24)
  • 3
    • 0029913459 scopus 로고    scopus 로고
    • Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration
    • (1996) J. Biol. Chem. , vol.271 , pp. 5458-5463
    • Szeltner, Z.1    Polgar, L.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.