Sankaranarayanan, R. ; Biswal, B. K. ; Vijayan, M. (2005) A new relaxed state in horse methemoglobin characterized by crystallographic studies Proteins: Structure, Function, and Bioinformatics, 60 (3). pp. 547-551. ISSN 0887-3585
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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/prot.20...
Related URL: http://dx.doi.org/10.1002/prot.20510
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 horse hemoglobin. 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: | Article |
|---|---|
| Source: | Copyright of this article belongs to John Wiley and Sons. |
| Keywords: | Hemoglobin; X-ray Crystallography; Quaternary Association; Protein Hydration; Intersubunit Mobility; Allosteric Transition |
| ID Code: | 53897 |
| Deposited On: | 10 Aug 2011 09:35 |
| Last Modified: | 13 Jul 2012 08:54 |
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