Crystallization and X-ray diffraction data analysis of oxyhemoglobin-I from the catfish Liposarcus anisitsi (pisces)
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
27/05/2014
27/05/2014
01/12/1997
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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 |