Source: Biotechnology and Bioengineering. Unidade: IQ
Assunto: BIOQUÍMICA
ABNT
ALMEIDA, F C L e VALENTE, A P e CHAIMOVICH GURALNIK, Hernan. Stability and activity modulation of chymotrypsin in AOT reserved micelles by protein-interface interaction of ALPHA-chymotrypsin with a negative interface leads to cooperative breakage of a salt bridge that keeps the catalytic active conformation [ILe (16) - Asp(194)]. Biotechnology and Bioengineering, v. 59, p. 360-3, 1998Tradução . . Acesso em: 06 out. 2024.APA
Almeida, F. C. L., Valente, A. P., & Chaimovich Guralnik, H. (1998). Stability and activity modulation of chymotrypsin in AOT reserved micelles by protein-interface interaction of ALPHA-chymotrypsin with a negative interface leads to cooperative breakage of a salt bridge that keeps the catalytic active conformation [ILe (16) - Asp(194)]. Biotechnology and Bioengineering, 59, 360-3.NLM
Almeida FCL, Valente AP, Chaimovich Guralnik H. Stability and activity modulation of chymotrypsin in AOT reserved micelles by protein-interface interaction of ALPHA-chymotrypsin with a negative interface leads to cooperative breakage of a salt bridge that keeps the catalytic active conformation [ILe (16) - Asp(194)]. Biotechnology and Bioengineering. 1998 ; 59 360-3.[citado 2024 out. 06 ]Vancouver
Almeida FCL, Valente AP, Chaimovich Guralnik H. Stability and activity modulation of chymotrypsin in AOT reserved micelles by protein-interface interaction of ALPHA-chymotrypsin with a negative interface leads to cooperative breakage of a salt bridge that keeps the catalytic active conformation [ILe (16) - Asp(194)]. Biotechnology and Bioengineering. 1998 ; 59 360-3.[citado 2024 out. 06 ]