Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity (2003)
- Authors:
- USP affiliated author: POLIKARPOV, IGOR - IFSC
- School: IFSC
- Subjects: CRISTALOGRAFIA; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Journal of Molecular Biology
- ISSN: 0022-2836
- Volume/Número/Paginação/Ano: v. 334, n. 5, p. 1023-1041, Dec. 2003
-
ABNT
APARICIO, Ricardo e FERREIRA, Sérgio T. e POLIKARPOV, Igor. Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. Journal of Molecular Biology, v. 334, n. 5, p. 1023-1041, 2003Tradução . . Acesso em: 19 ago. 2022. -
APA
Aparicio, R., Ferreira, S. T., & Polikarpov, I. (2003). Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. Journal of Molecular Biology, 334( 5), 1023-1041. -
NLM
Aparicio R, Ferreira ST, Polikarpov I. Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. Journal of Molecular Biology. 2003 ; 334( 5): 1023-1041.[citado 2022 ago. 19 ] -
Vancouver
Aparicio R, Ferreira ST, Polikarpov I. Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. Journal of Molecular Biology. 2003 ; 334( 5): 1023-1041.[citado 2022 ago. 19 ] - Crystallization and preliminary estudies of the ligand binding domain (LBD) of the nuclear receptor NGFI-B
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