Crystallization and X-ray diffraction data analysis of oxyhemoglobin-I from the catfish Liposarcus anisitsi (pisces)


Autoria(s): Smarra, A. L S; Arni, R. K.; De Azevedo, W. F.; Colombo, M. F.; Bonilla-Rodriguez, G. O.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

27/05/2014

27/05/2014

01/12/1997

Resumo

Hemoglobin remains, despite the enormous amount of research involving this molecule, as a prototype for allosteric models and new conformations. Functional studies carried out on Hemoglobin-I from the South-American Catfish Liposarcus anisitsi [1] suggest the existence of conformational states beyond those already described for human hemoglobin, which could be confirmed crystallographically. The present work represents the initial steps towards that goal.

Formato

349-354

Identificador

Protein and Peptide Letters, v. 4, n. 5, p. 349-354, 1997.

0929-8665

http://hdl.handle.net/11449/65330

2-s2.0-0001384330

Idioma(s)

eng

Relação

Protein and Peptide Letters

Direitos

closedAccess

Tipo

info:eu-repo/semantics/article