Source:http://linkedlifedata.com/resource/pubmed/id/19266317
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
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| pubmed:dateCreated |
2010-2-10
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| pubmed:abstractText |
C-H....pi interactions are known to be important contributors to protein stability. In this study, we have analyzed the influence of C-H....pi interactions in single chain "all-alpha" proteins. In the data set, a total of 181 C-H....pi interactions were observed. The most prominent representatives are the interactions between aromatic C-H donor groups and aromatic pi acceptors. Eighty-one percent of the C-H....pi interactions between side chain to side chain and remaining19% of the C-H....pi interactions were observed between side-chain to side-chain five-member aromatic ring. The donor atom contribution to C-H....pi interactions was mainly from Phe, Tyr, and Trp residues. The acceptor atom contribution to C-H....pi interactions was mainly from Phe, Tyr, Trp, and His. The highest percentage of C-H....pi interactions were observed form Phe residue. The secondary structure preference analysis of all C-H....pi interacting residues showed that Phe, Tyr, Trp, and His preferred to be in helix. Long-range C-H....pi interactions are the predominant type of interactions in single chain all-alpha proteins data set. All the C-H....pi interactions forming residues in the data set preferred to be in the buried region. Seventy-three percent of the donor residues and 65% of the acceptor residues are highly conserved.
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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 |
Mar
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| pubmed:issn |
1559-0291
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
160
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1473-83
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| pubmed:meshHeading | |
| pubmed:year |
2010
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| pubmed:articleTitle |
Exploring the role of C-H....pi interactions on the structural stability of single chain "all-alpha" proteins.
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| pubmed:affiliation |
School of Biotechnology, Chemical and Biomedical Engineering, Bioinformatics Division, Vellore Institute of Technology, Vellore 632014, Tamil Nadu, India.
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| pubmed:publicationType |
Journal Article
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