Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties. Export

@article{citeulike:467316, abstract = {In the present work, we use structural information to characterize a set of disease-associated single amino acid polymorphisms exhaustively. The analysis of different properties, such as substitution matrix elements, secondary structure, accessibility, free energies of transfer from water to octanol, amino acid volume, etc., suggests that many disease-causing mutations are associated with extreme changes in the value of parameters relating to protein stability. Overall, our results indicate that, while knowledge of protein structure clearly helps in understanding these mutations, a finer understanding can come only from a quantitative knowledge of protein stability and of the protein environment in the cell. Interestingly, use of evolutionary information from multiple sequence alignments can be used to increase our knowledge of disease-associated mutations.}, address = {Departament de Bioqu\'{\i}mica i Biologia Molecular, Facultat de Qu\'{\i}mica, Universitat de Barcelona, Spain.}, author = {Ferrer-Costa, Carles and Orozco, Modesto and de la Cruz, Xavier}, citeulike-article-id = {467316}, citeulike-linkout-0 = {http://dx.doi.org/10.1006/jmbi.2001.5255}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11812146}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11812146}, citeulike-linkout-3 = {http://www.sciencedirect.com/science/article/B6WK7-4576DCM-1D/2/c2430087bdfd491b9419d5c9a25bcc4a}, day = {25}, doi = {10.1006/jmbi.2001.5255}, issn = {0022-2836}, journal = {Journal of molecular biology}, keywords = {comps, function, major-proposal}, month = {January}, number = {4}, pages = {771--786}, posted-at = {2006-09-14 01:23:57}, priority = {5}, title = {Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties.}, url = {http://dx.doi.org/10.1006/jmbi.2001.5255}, volume = {315}, year = {2002} }

TY - JOUR ID - citeulike:467316 L3 - citeulike-article-id:467316 N2 - In the present work, we use structural information to characterize a set of disease-associated single amino acid polymorphisms exhaustively. The analysis of different properties, such as substitution matrix elements, secondary structure, accessibility, free energies of transfer from water to octanol, amino acid volume, etc., suggests that many disease-causing mutations are associated with extreme changes in the value of parameters relating to protein stability. Overall, our results indicate that, while knowledge of protein structure clearly helps in understanding these mutations, a finer understanding can come only from a quantitative knowledge of protein stability and of the protein environment in the cell. Interestingly, use of evolutionary information from multiple sequence alignments can be used to increase our knowledge of disease-associated mutations. IS - 4 JF - Journal of molecular biology SN - 0022-2836 AD - Departament de Bioquímica i Biologia Molecular, Facultat de Química, Universitat de Barcelona, Spain. EP - 786 TI - Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties. VL - 315 SP - 771 KW - comps KW - function KW - major-proposal AU - Ferrer-Costa, Carles AU - Orozco, Modesto AU - de la Cruz, Xavier PY - 2002/01/25/ UR - http://dx.doi.org/10.1006/jmbi.2001.5255 ER -