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A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase.

Abstract:

The denaturation of triose phosphate isomerase (TIM) from Saccharomyces cerevisiae by guanidine hydrochlorids at pH 7.2 has been monitored by NMR spectroscopy in conjunction with optical spectroscopy. In the absence of denaturant, the hydrodynamic radius of 29.6(+/-0.25) A and the substantial chemical shift dispersion evident in the NMR spectrum are consistent with the highly structured dimeric native state of the protein. On the addition of 2. 2 M guanidine hydrochloride the effective hydrod...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.2000.3834

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Journal of molecular biology
Volume:
300
Issue:
1
Pages:
11-16
Publication date:
2000-06-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:d9b137f2-bcad-4170-99f3-2bd58083a353
Source identifiers:
31705
Local pid:
pubs:31705

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