A new relaxed state in horse methemoglobin characterized by crystallographic studies

Sankaranarayanan, R and Biswal, BK and Vijayan, M (2005) A new relaxed state in horse methemoglobin characterized by crystallographic studies. In: Proteins: Structure, Function, and Bioinformatics, 60 (3). pp. 547-551.

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Abstract

A new relaxed state has been characterized in the crystals of horse methemoglobin grown at neutral pH at low ionic concentration and their low humidity variants. The crystals provide an example for improvement in X-ray diffraction quality with reduced solvent content. Only the classical R state has been so far observed in liganded horsehemoglobin. The state characterized in the present study lies in between the R state and the R2 state characterized earlier in liganded human hemoglobin. The results presented here, along with those of earlier studies, suggest that relaxed and tense hemoglobin can access ensembles of states.

Item Type:	Journal Article
Publication:	Proteins: Structure, Function, and Bioinformatics
Publisher:	Wiley-Liss
Additional Information:	Copyright for this article belongs to Wiley-Liss.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	02 Sep 2005
Last Modified:	19 Sep 2010 04:20
URI:	http://eprints.iisc.ac.in/id/eprint/3603

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