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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
36
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pubmed:dateCreated |
2000-10-13
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pubmed:abstractText |
31P NMR spectroscopy has been used to show that the activity of RNase A, which is lowered in the presence of urea, can be recovered with trimethylamine-N-oxide (TMAO). A 1:1 ratio of TMAO:urea was sufficient to recover the enzyme activity. (1)H nuclear Overhauser effect spectroscopy NMR studies with RNase A have shown that even at relatively low effective concentrations of TMAO, some modification of the three-dimensional structure of the biomolecule is apparent.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27708-11
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10862769-Animals,
pubmed-meshheading:10862769-Cattle,
pubmed-meshheading:10862769-Hydrogen,
pubmed-meshheading:10862769-Methylamines,
pubmed-meshheading:10862769-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:10862769-Oxidants,
pubmed-meshheading:10862769-Phosphorus,
pubmed-meshheading:10862769-Poly U,
pubmed-meshheading:10862769-Protein Conformation,
pubmed-meshheading:10862769-Ribonuclease, Pancreatic,
pubmed-meshheading:10862769-Urea
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pubmed:year |
2000
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pubmed:articleTitle |
31P and 1H NMR studies of the effect of the counteracting osmolyte trimethylamine-N-oxide on interactions of urea with ribonuclease A.
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pubmed:affiliation |
Department of Physiology, University of Otago Medical School and the Department of Chemistry, University of Otago, Dunedin 9001, New Zealand.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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