How frequent are correlated changes in families of protein sequences?

@article{citeulike:875168, abstract = {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.}, address = {Max-Planck-Institut f\"{u}r Biophysikalische Chemie, Abteilung Membranbiophysik, G\"{o}ttingen, Federal Republic of Germany.}, author = {Neher, E. }, citeulike-article-id = {875168}, doi = {http://dx.doi.org/10.1073/pnas.91.1.98}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, month = {January}, number = {1}, pages = {98--102}, posted-at = {2006-09-27 07:34:38}, priority = {2}, title = {How frequent are correlated changes in families of protein sequences?}, url = {http://dx.doi.org/10.1073/pnas.91.1.98}, volume = {91}, year = {1994} }

TY - JOUR ID - citeulike:875168 L3 - citeulike-article-id:875168 TI - How frequent are correlated changes in families of protein sequences? JF - Proc Natl Acad Sci U S A VL - 91 IS - 1 SP - 98 EP - 102 AD - Max-Planck-Institut für Biophysikalische Chemie, Abteilung Membranbiophysik, Göttingen, Federal Republic of Germany. SN - 0027-8424 N2 - 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. AU - Neher, E PY - 1994/01/04/ UR - http://dx.doi.org/10.1073/pnas.91.1.98 ER -