Source:http://linkedlifedata.com/resource/pubmed/id/18851941
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-12-19
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1096-0384
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
481
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
52-8
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pubmed:meshHeading |
pubmed-meshheading:18851941-Amino Acid Sequence,
pubmed-meshheading:18851941-Archaeal Proteins,
pubmed-meshheading:18851941-Circular Dichroism,
pubmed-meshheading:18851941-Kinetics,
pubmed-meshheading:18851941-Models, Molecular,
pubmed-meshheading:18851941-Molecular Sequence Data,
pubmed-meshheading:18851941-Mutation,
pubmed-meshheading:18851941-Protein Conformation,
pubmed-meshheading:18851941-Protein Folding,
pubmed-meshheading:18851941-Static Electricity,
pubmed-meshheading:18851941-Thermodynamics
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pubmed:year |
2009
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pubmed:articleTitle |
Favorable contribution of the C-terminal residue K97 to the stability of a hyperthermophilic archaeal [P62A]Ssh10b.
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pubmed:affiliation |
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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