NMR studies of protein surface accessibility.

@article{citeulike:637249, abstract = {Characterization of protein surface accessibility represents a new frontier of structural biology. A surface accessibility investigation for two structurally well-defined proteins, tendamistat and bovine pancreatic trypsin inhibitor, is performed here by a combined analysis of water-protein Overhauser effects and paramagnetic perturbation profiles induced by the soluble spin-label 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl on NMR spectra. This approach seems to be reliable not only for distinguishing between buried and exposed residues but also for finding molecular locations where a network of more ordered waters covers the protein surface. From the presented set of data, an overall picture of the surface accessibility of the two proteins can be inferred. Detailed knowledge of protein accessibility can form the basis for successful design of mutants with increased activity and/or greater specificity.}, address = {Biomolecular Structure Research Center and Department of Molecular Biology, University of Siena, I-53100 Siena, Italy.}, author = {Niccolai, N. and Ciutti, A. and Spiga, O. and Scarselli, M. and Bernini, A. and Bracci, L. and Di Maro, D. and Dalvit, C. and Molinari, H. and Esposito, G. and Temussi, P. A. }, citeulike-article-id = {637249}, doi = {10.1074/jbc.M107387200}, issn = {0021-9258}, journal = {J Biol Chem}, keywords = {41062062, ambiente, contaminacion, medio}, month = {November}, number = {45}, pages = {42455--42461}, posted-at = {2007-05-11 22:39:00}, priority = {2}, title = {NMR studies of protein surface accessibility.}, url = {http://dx.doi.org/10.1074/jbc.M107387200}, volume = {276}, year = {2001} }

TY - JOUR ID - citeulike:637249 L3 - citeulike-article-id:637249 TI - NMR studies of protein surface accessibility. JF - J Biol Chem VL - 276 IS - 45 SP - 42455 EP - 42461 AD - Biomolecular Structure Research Center and Department of Molecular Biology, University of Siena, I-53100 Siena, Italy. SN - 0021-9258 N2 - Characterization of protein surface accessibility represents a new frontier of structural biology. A surface accessibility investigation for two structurally well-defined proteins, tendamistat and bovine pancreatic trypsin inhibitor, is performed here by a combined analysis of water-protein Overhauser effects and paramagnetic perturbation profiles induced by the soluble spin-label 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl on NMR spectra. This approach seems to be reliable not only for distinguishing between buried and exposed residues but also for finding molecular locations where a network of more ordered waters covers the protein surface. From the presented set of data, an overall picture of the surface accessibility of the two proteins can be inferred. Detailed knowledge of protein accessibility can form the basis for successful design of mutants with increased activity and/or greater specificity. KW - 41062062 KW - ambiente KW - contaminacion KW - medio AU - Niccolai, N AU - Ciutti, A AU - Spiga, O AU - Scarselli, M AU - Bernini, A AU - Bracci, L AU - Di Maro, D AU - Dalvit, C AU - Molinari, H AU - Esposito, G AU - Temussi, PA PY - 2001/11/09/ UR - http://dx.doi.org/10.1074/jbc.M107387200 ER -