| pubmed-article:17335845 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17335845 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:17335845 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:17335845 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:17335845 | lifeskim:mentions | umls-concept:C0598629 | lld:lifeskim |
| pubmed-article:17335845 | lifeskim:mentions | umls-concept:C0006407 | lld:lifeskim |
| pubmed-article:17335845 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:17335845 | lifeskim:mentions | umls-concept:C0205324 | lld:lifeskim |
| pubmed-article:17335845 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17335845 | pubmed:dateCreated | 2007-3-26 | lld:pubmed |
| pubmed-article:17335845 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:abstractText | Formation of a flat beta-sheet is a fundamental event in beta-sheet-mediated protein self-assembly. To investigate the contributions of various factors to the stability of flat beta-sheets, we performed extensive alanine-scanning mutagenesis experiments on the single-layer beta-sheet segment of Borrelia outer surface protein A (OspA). This beta-sheet segment consists of beta-strands with highly regular geometries that can serve as a building block for self-assembly. Our Ala-scanning approach is distinct from the conventional host-guest method, in that it introduces only conservative, truncation mutations that should minimize structural perturbation. Our results showed very weak correlation with experimental beta-sheet propensity scales, statistical beta-sheet propensity scales, or cross-strand pairwise correlations. In contrast, our data showed strong positive correlation with the change in buried non-polar surface area. Polar interactions including prominent Glu-Lys cross-strand pairs contribute marginally to the beta-sheet stability. These results were corroborated by results from additional non-Ala mutations. Taken together, these results demonstrate the dominant contribution of non-polar surface burial to flat beta-sheet stability even at solvent-exposed positions. The OspA single-layer beta-sheet achieves efficient hydrophobic surface burial without forming a hydrophobic core by a strategic placement of a variety of side-chains. These findings further suggest the importance of hydrophobic interactions within a beta-sheet layer in peptide self-assembly. | lld:pubmed |
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| pubmed-article:17335845 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17335845 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17335845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17335845 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335845 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17335845 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17335845 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:17335845 | pubmed:author | pubmed-author:KoideAkikoA | lld:pubmed |
| pubmed-article:17335845 | pubmed:author | pubmed-author:KoideShoheiS | lld:pubmed |
