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1vrf

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[[Image:1vrf.gif|left|200px]]
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{{STRUCTURE_1vrf| PDB=1vrf | SCENE= }}
{{STRUCTURE_1vrf| PDB=1vrf | SCENE= }}
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'''SOLUTION STRUCTURE OF COMPONENT IV GLYCERA DIBRANCHIATA MONOMERIC HEMOGLOBIN-CO'''
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===SOLUTION STRUCTURE OF COMPONENT IV GLYCERA DIBRANCHIATA MONOMERIC HEMOGLOBIN-CO===
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==Overview==
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The solution structure and backbone dynamics of the recombinant, ferrous CO-ligated form of component IV monomeric hemoglobin from Glycera dibranchiata (GMH4CO) have been characterized by NMR spectroscopy. Distance geometry and simulated annealing calculations utilizing a total of 2550 distance and torsion angle constraints yielded an ensemble of 29 structures with an overall average backbone rmsd of 0.48 A from the average structure. Differences between the solution structure and a related crystal structure are confined to regions of lower precision in either the NMR or X-ray structure, or in regions where the amino acid sequences differ. 15N relaxation measurements at 76.0 and 60.8 MHz were analyzed with an extended model-free approach, and revealed low-frequency motions in the vicinity of the heme, concentrated in the F helix. Amide proton protection factors were obtained from H-D amide exchange measurements on 15N-labeled protein. Patterns in the backbone dynamics and protection factors were shown to correlate with regions of heterogeneity and disorder in the ensemble of NMR structures and with large crystallographic B-factors in the X-ray structures. Surprisingly, while the backbone atoms of the F helix have higher rmsds and larger measures of dynamics on the microsecond to millisecond time scale than the other helices, amide protection factors for residues in the F helix were observed to be similar to those of the other helices. This contrasts with H-D amide exchange measurements on sperm whale myoglobin which indicated low protection for the F helix (S. N. Loh and B. F. Volkman, unpublished results). These results for GMH4 suggest a model in which the F helix undergoes collective motions as a relatively rigid hydrogen-bonded unit, possibly pivoting about a central position near residue Val87.
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(as it appears on PubMed at http://www.pubmed.gov), where 9692983 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9692983}}
==About this Structure==
==About this Structure==
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1VRF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycera_dibranchiata Glycera dibranchiata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRF OCA].
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1VRF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycera_dibranchiata Glycera dibranchiata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRF OCA].
==Reference==
==Reference==
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[[Category: Heme protein]]
[[Category: Heme protein]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:50:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:19:53 2008''

Revision as of 10:19, 27 July 2008

Image:1vrf.png

Template:STRUCTURE 1vrf

SOLUTION STRUCTURE OF COMPONENT IV GLYCERA DIBRANCHIATA MONOMERIC HEMOGLOBIN-CO

Template:ABSTRACT PUBMED 9692983

About this Structure

1VRF is a Single protein structure of sequence from Glycera dibranchiata. Full experimental information is available from OCA.

Reference

Solution structure and backbone dynamics of component IV Glycera dibranchiata monomeric hemoglobin-CO., Volkman BF, Alam SL, Satterlee JD, Markley JL, Biochemistry. 1998 Aug 4;37(31):10906-19. PMID:9692983

Page seeded by OCA on Sun Jul 27 13:19:53 2008

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