| pubmed-article:8278414 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8278414 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:8278414 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:8278414 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:8278414 | lifeskim:mentions | umls-concept:C1707520 | lld:lifeskim |
| pubmed-article:8278414 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:8278414 | lifeskim:mentions | umls-concept:C0332183 | lld:lifeskim |
| pubmed-article:8278414 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8278414 | pubmed:dateCreated | 1994-2-4 | lld:pubmed |
| pubmed-article:8278414 | pubmed:abstractText | A loss-of-function point mutation in a protein is often rescued by an additional mutation that compensates for the original physical change. According to one hypothesis, such compensation would be most effective in maintaining a structural motif if the two mutated residues were spatial neighbors. If this hypothesis were correct, one would expect that many such compensatory mutations have occurred during evolution and that present-day protein families show some degree of correlation in the occurrence of amino acid residues at positions whose side chains are in contact. Here, a statistical theory is presented which allows evaluation of correlations in a family of aligned protein sequences by assigning a scalar metric (such as charge or side-chain volume) to each type of amino acid and calculating correlation coefficients of these quantities at different positions. For the family of myoglobins it is found that there is a high correlation between fluctuations in neighboring charges. The correlation is close to what would be expected for total conservation of local charge. For the metric side-chain volume, on the other hand, no correlation could be found. | lld:pubmed |
| pubmed-article:8278414 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8278414 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8278414 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8278414 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8278414 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8278414 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8278414 | pubmed:author | pubmed-author:NeherEE | lld:pubmed |
| pubmed-article:8278414 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8278414 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:8278414 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:8278414 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8278414 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8278414 | pubmed:pagination | 98-102 | lld:pubmed |
| pubmed-article:8278414 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:meshHeading | pubmed-meshheading:8278414-... | lld:pubmed |
| pubmed-article:8278414 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8278414 | pubmed:articleTitle | How frequent are correlated changes in families of protein sequences? | lld:pubmed |
| pubmed-article:8278414 | pubmed:affiliation | Max-Planck-Institut für Biophysikalische Chemie, Abteilung Membranbiophysik, Göttingen, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:8278414 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8278414 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8278414 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8278414 | lld:pubmed |
