The hypervariable D3 domain of Salmonella flagellin is an autonomous folding unit. Export

@article{citeulike:3079645, abstract = {The hypervariable D3 domain of Salmonella flagellin, composed of the 190-285 segment, is the major determinant of flagellar antigenicity. D3 was cloned and overexpressed in E. coli. Although previous studies concluded that D3 is stabilized by interactions with the D2 domain, our calorimetric experiments have revealed that isolated D3 has a stable tertiary structure which is highly resistant against proteolytic digestion. Repeated heating experiments demonstrated that unfolding of D3 is reversible. Its small size and stable structure makes D3 a promising protein scaffold for the development of artificial binding proteins by directed evolution.}, address = {Research Institute for Technical Physics and Materials Science, Hungarian Academy of Sciences, Konkoly Thege u. 29-33, H-1121 Budapest, Hungary.}, author = {Sebesty\'{e}n, A. and Muskot\'{a}l, A. and V\'{e}gh, B. M. and Vonderviszt, F.}, citeulike-article-id = {3079645}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/18221014}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=18221014}, issn = {0929-8665}, journal = {Protein and peptide letters}, keywords = {flagellar}, number = {1}, pages = {54--57}, posted-at = {2008-08-04 08:18:13}, priority = {3}, title = {The hypervariable D3 domain of Salmonella flagellin is an autonomous folding unit.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/18221014}, volume = {15}, year = {2008} }

TY - JOUR ID - citeulike:3079645 L3 - citeulike-article-id:3079645 N2 - The hypervariable D3 domain of Salmonella flagellin, composed of the 190-285 segment, is the major determinant of flagellar antigenicity. D3 was cloned and overexpressed in E. coli. Although previous studies concluded that D3 is stabilized by interactions with the D2 domain, our calorimetric experiments have revealed that isolated D3 has a stable tertiary structure which is highly resistant against proteolytic digestion. Repeated heating experiments demonstrated that unfolding of D3 is reversible. Its small size and stable structure makes D3 a promising protein scaffold for the development of artificial binding proteins by directed evolution. IS - 1 JF - Protein and peptide letters SN - 0929-8665 AD - Research Institute for Technical Physics and Materials Science, Hungarian Academy of Sciences, Konkoly Thege u. 29-33, H-1121 Budapest, Hungary. EP - 57 TI - The hypervariable D3 domain of Salmonella flagellin is an autonomous folding unit. VL - 15 SP - 54 KW - flagellar AU - Sebestyén, A AU - Muskotál, A AU - Végh, BM AU - Vonderviszt, F PY - 2008/// UR - http://view.ncbi.nlm.nih.gov/pubmed/18221014 ER -