Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1994-2-4
|
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.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8278414-1377638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8278414-2017436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8278414-3018752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8278414-3237684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8278414-3612789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8278414-3709526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8278414-5555208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8278414-7373651
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0027-8424
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
4
|
pubmed:volume |
91
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
98-102
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:8278414-Amino Acid Sequence,
pubmed-meshheading:8278414-Animals,
pubmed-meshheading:8278414-Mutation,
pubmed-meshheading:8278414-Myoglobin,
pubmed-meshheading:8278414-Protein Conformation,
pubmed-meshheading:8278414-Sequence Alignment,
pubmed-meshheading:8278414-Sequence Analysis,
pubmed-meshheading:8278414-Sequence Homology, Amino Acid,
pubmed-meshheading:8278414-Structure-Activity Relationship
|
pubmed:year |
1994
|
pubmed:articleTitle |
How frequent are correlated changes in families of protein sequences?
|
pubmed:affiliation |
Max-Planck-Institut für Biophysikalische Chemie, Abteilung Membranbiophysik, Göttingen, Federal Republic of Germany.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|