| pubmed-article:7663349 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7663349 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
| pubmed-article:7663349 | lifeskim:mentions | umls-concept:C0079866 | lld:lifeskim |
| pubmed-article:7663349 | lifeskim:mentions | umls-concept:C0039808 | lld:lifeskim |
| pubmed-article:7663349 | lifeskim:mentions | umls-concept:C0020276 | lld:lifeskim |
| pubmed-article:7663349 | lifeskim:mentions | umls-concept:C0877853 | lld:lifeskim |
| pubmed-article:7663349 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7663349 | pubmed:dateCreated | 1995-10-10 | lld:pubmed |
| pubmed-article:7663349 | pubmed:abstractText | Anomalous NMR behavior of the hydroxyl proton resonance for Ser 31 has been reported for histidine-containing protein (HPr) from two microorganisms: Escherichia coli and Staphylococcus aureus. The unusual slow exchange and chemical shift exhibited by the resonance led to the proposal that the hydroxyl group is involved in a strong hydrogen bond. To test this hypothesis and to characterize the importance of such an interaction, a mutant in which Ser 31 is replaced by an alanine was generated in HPr from Escherichia coli. The activity, stability, and structure of the mutant HPr were assessed using a reconstituted assay system, analysis of solvent denaturation curves, and NMR, respectively. Substitution of Ser 31 yields a fully functional protein that is only slightly less stable (delta delta G(folding) = 0.46 +/- 0.15 kcal mol-1) than the wild type. The NMR results confirm the identity of the hydrogen bond acceptor as Asp 69 and reveal that it exists as the gauche- conformer in wild-type HPr in solution but exhibits conformational averaging in the mutant protein. The side chain of Asp 69 interacts with two main-chain amide proteins in addition to its interaction with the side chain of Ser 31 in the wild-type protein. These results indicate that removal of the serine has led to the loss of all three hydrogen bond interactions involving Asp 69, suggesting a cooperative network of interactions. A complete analysis of the thermodynamics was performed in which differences in side-chain hydrophobicity and conformational entropy between the two proteins are accounted for.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
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| pubmed-article:7663349 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7663349 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7663349 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7663349 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7663349 | pubmed:month | May | lld:pubmed |
| pubmed-article:7663349 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:7663349 | pubmed:author | pubmed-author:AndersonJ WJW | lld:pubmed |
| pubmed-article:7663349 | pubmed:author | pubmed-author:WaygoodE BEB | lld:pubmed |
| pubmed-article:7663349 | pubmed:author | pubmed-author:KlevitR ERE | lld:pubmed |
| pubmed-article:7663349 | pubmed:author | pubmed-author:ScholtzJ MJM | lld:pubmed |
| pubmed-article:7663349 | pubmed:author | pubmed-author:HammenP KPK | lld:pubmed |
| pubmed-article:7663349 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7663349 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:7663349 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7663349 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7663349 | pubmed:pagination | 936-44 | lld:pubmed |
| pubmed-article:7663349 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7663349 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7663349 | pubmed:articleTitle | Investigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopy. | lld:pubmed |
| pubmed-article:7663349 | pubmed:affiliation | Department of Biochemistry, University of Washington, Seattle 98195, USA. | lld:pubmed |
| pubmed-article:7663349 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7663349 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7663349 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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