| pubmed-article:11262940 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11262940 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:11262940 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11262940 | lifeskim:mentions | umls-concept:C0015219 | lld:lifeskim |
| pubmed-article:11262940 | lifeskim:mentions | umls-concept:C0019409 | lld:lifeskim |
| pubmed-article:11262940 | pubmed:dateCreated | 2001-3-23 | lld:pubmed |
| pubmed-article:11262940 | pubmed:abstractText | New computational models of the kinetics of natural site substitutions in proteins are described based on the underlying physical chemical properties of the amino acids. The corresponding reduction in the number of adjustable parameters allows us to analyze site-heterogeneity. Applying this evolutionary model to various data sets allows us to identify the important factors constraining molecular evolution, providing insight into the relationship between amino acid properties and protein structure. | lld:pubmed |
| pubmed-article:11262940 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11262940 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11262940 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11262940 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11262940 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11262940 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11262940 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11262940 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11262940 | pubmed:issn | 1793-5091 | lld:pubmed |
| pubmed-article:11262940 | pubmed:author | pubmed-author:GoldsteinR... | lld:pubmed |
| pubmed-article:11262940 | pubmed:author | pubmed-author:KoshiJ MJM | lld:pubmed |
| pubmed-article:11262940 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11262940 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11262940 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11262940 | pubmed:pagination | 191-202 | lld:pubmed |
| pubmed-article:11262940 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:11262940 | pubmed:meshHeading | pubmed-meshheading:11262940... | lld:pubmed |
| pubmed-article:11262940 | pubmed:meshHeading | pubmed-meshheading:11262940... | lld:pubmed |
| pubmed-article:11262940 | pubmed:meshHeading | pubmed-meshheading:11262940... | lld:pubmed |
| pubmed-article:11262940 | pubmed:meshHeading | pubmed-meshheading:11262940... | lld:pubmed |
| pubmed-article:11262940 | pubmed:meshHeading | pubmed-meshheading:11262940... | lld:pubmed |
| pubmed-article:11262940 | pubmed:meshHeading | pubmed-meshheading:11262940... | lld:pubmed |
| pubmed-article:11262940 | pubmed:meshHeading | pubmed-meshheading:11262940... | lld:pubmed |
| pubmed-article:11262940 | pubmed:meshHeading | pubmed-meshheading:11262940... | lld:pubmed |
| pubmed-article:11262940 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11262940 | pubmed:articleTitle | Analyzing site heterogeneity during protein evolution. | lld:pubmed |
| pubmed-article:11262940 | pubmed:affiliation | Biophysics Research Division, University of Michigan, Ann Arbor, MI 48109-1055, USA. | lld:pubmed |
| pubmed-article:11262940 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11262940 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11262940 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11262940 | lld:pubmed |
