- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1006/jmbi.2000.3834
-
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- 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
- Copyright date:
- 2000
Journal article
A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase.
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