PubMed · 11546818
NMR studies of protein surface accessibility.
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.
Explore related subjects
Keep this discovery
Explore connections, maps & timelines
N Niccolai, A Ciutti, O Spiga, M Scarselli, A Bernini, L Bracci, D Di Maro, C Dalvit, H Molinari, G Esposito, P A Temussi. 2001-09-06. NMR studies of protein surface accessibility.. https://doi.org/10.1074/jbc.m107387200
Cite the original work for its findings. Save a collection to share your selection of sources.