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)] (1998)
- Authors:
- Autor USP: GURALNIK, HERNAN CHAIMOVICH - IQ
- Unidade: IQ
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Biotechnology and Bioengineering
- Volume/Número/Paginação/Ano: v. 59, p. 360-3, 1998
-
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: 27 jul. 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 jul. 27 ] -
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 jul. 27 ] - Micelar and vesicular effects on reaction mechanisms
- Peg changes the fusion pattern in the case of unmodified fusogenic peptides
- Effect of detergents and other amphiphiles on the stability of pharmaceutical drugs
- Effect of the treatment with neuraminidase the behavior of alkaline phosphatase in micelles
- Sera from patients with chronic chagas' disease may exhibit anti-cardiolipin activity
- 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)]
- `Beta´-2-glycoprotein I induces leakage from cardioliopin-containing vesicles by a non-fusion mechanism: binding, bilayer unsteady, aggregation and leakage
- Estrutura e reatividade em micelas
- Autonomia?
- Entrevista com o Prof. Hernan Chaimovich
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
