| pubmed-article:20609364 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20609364 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:20609364 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:20609364 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:20609364 | lifeskim:mentions | umls-concept:C1512665 | lld:lifeskim |
| pubmed-article:20609364 | lifeskim:mentions | umls-concept:C0679083 | lld:lifeskim |
| pubmed-article:20609364 | lifeskim:mentions | umls-concept:C1999230 | lld:lifeskim |
| pubmed-article:20609364 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:20609364 | pubmed:dateCreated | 2010-8-2 | lld:pubmed |
| pubmed-article:20609364 | pubmed:abstractText | Cel9A from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius belongs to the subfamily E1 of family 9 glycoside hydrolases, many members of which have an N-terminal Ig-like domain followed by the catalytic domain. The Ig-like domain is not directly involved in either carbohydrate binding or biocatalysis; however, deletion of the Ig-domain promotes loss of enzymatic activity. We have investigated the functional role of the Ig-like domain using molecular dynamics simulations. Our simulations indicate that residues within the Ig-like domain are dynamically correlated with residues in the carbohydrate-binding pocket and with key catalytic residues of Cel9A. Free energy perturbation simulations indicate that the Ig-like domain stabilizes the catalytic domain and may be responsible for the enhanced thermostability of Cel9A. | lld:pubmed |
| pubmed-article:20609364 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20609364 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20609364 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20609364 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20609364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20609364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20609364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20609364 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20609364 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:20609364 | pubmed:issn | 1873-3468 | lld:pubmed |
| pubmed-article:20609364 | pubmed:author | pubmed-author:AdamsPaul DPD | lld:pubmed |
| pubmed-article:20609364 | pubmed:author | pubmed-author:SaleKenneth... | lld:pubmed |
| pubmed-article:20609364 | pubmed:author | pubmed-author:SapraRajatR | lld:pubmed |
| pubmed-article:20609364 | pubmed:author | pubmed-author:SimmonsBlake... | lld:pubmed |
| pubmed-article:20609364 | pubmed:author | pubmed-author:LiuHanbinH | lld:pubmed |
| pubmed-article:20609364 | pubmed:author | pubmed-author:PereiraJose... | lld:pubmed |
| pubmed-article:20609364 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20609364 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:20609364 | pubmed:volume | 584 | lld:pubmed |
| pubmed-article:20609364 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20609364 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20609364 | pubmed:pagination | 3431-5 | lld:pubmed |
| pubmed-article:20609364 | pubmed:dateRevised | 2010-10-25 | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:meshHeading | pubmed-meshheading:20609364... | lld:pubmed |
| pubmed-article:20609364 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20609364 | pubmed:articleTitle | Molecular simulations provide new insights into the role of the accessory immunoglobulin-like domain of Cel9A. | lld:pubmed |
| pubmed-article:20609364 | pubmed:affiliation | Deconstruction Division, Joint BioEnergy Institute, Emeryville, CA, United States. | lld:pubmed |
| pubmed-article:20609364 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20609364 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20609364 | lld:entrezgene |
