| pubmed-article:18851941 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18851941 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:18851941 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:18851941 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:18851941 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:18851941 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18851941 | pubmed:dateCreated | 2008-12-19 | lld:pubmed |
| pubmed-article:18851941 | pubmed:abstractText | The role of residue K97 at the C-terminal end of archaeal [P62A]Ssh10b in the hyperthermostability of the protein is investigated using three K97-mutant variants: K97E-, K97A-, and DeltaK97-mutant [P62A]Ssh10b. The thermal- and GdmHCl-induced denaturation of the three mutant variants has been monitored by circular dichroism. The results reveal that the K97E mutation leads to a stronger destabilization effect than the K97A mutation by disturbing the electrostatic interaction of the salt-bridge D63-K97 and drawing an unfavorable charge-charge repulsive interaction into the structure. However, DeltaK97-[P62A]Ssh10b shows much lower stability than K97E- and K97A-mutant [P62A]Ssh10b. Analysis suggests that residue K97 at the C-terminal end makes the favorable contributions to the stability of hyperthermophilic [P62A]Ssh10b not only by the favorable electrostatic interactions with residues in close vicinity but also through maintaining the side chain packing of the surrounding residues in the C-terminal area of the protein. | lld:pubmed |
| pubmed-article:18851941 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18851941 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18851941 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18851941 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18851941 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18851941 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:18851941 | pubmed:issn | 1096-0384 | lld:pubmed |
| pubmed-article:18851941 | pubmed:author | pubmed-author:WangJinfengJ | lld:pubmed |
| pubmed-article:18851941 | pubmed:author | pubmed-author:FengYingangY | lld:pubmed |
| pubmed-article:18851941 | pubmed:author | pubmed-author:FangXianyangX | lld:pubmed |
| pubmed-article:18851941 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18851941 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:18851941 | pubmed:volume | 481 | lld:pubmed |
| pubmed-article:18851941 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18851941 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18851941 | pubmed:pagination | 52-8 | lld:pubmed |
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| pubmed-article:18851941 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:18851941 | pubmed:articleTitle | Favorable contribution of the C-terminal residue K97 to the stability of a hyperthermophilic archaeal [P62A]Ssh10b. | lld:pubmed |
| pubmed-article:18851941 | pubmed:affiliation | National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China. | lld:pubmed |
| pubmed-article:18851941 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18851941 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18851941 | lld:pubmed |
