Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4565
Title: NMR studies of protein surface accessibility.
Authors: Niccolai, Neri 
Ciutti, A
Spiga, Ottavia 
Scarselli, M
Bernini, A
Bracci, Luisa
DI MARO, D
Dalvit, C
Molinari, H
Esposito, G
Temussi, Pa
Issue Date: 2001
Project: None 
Journal: THE JOURNAL OF BIOLOGICAL CHEMISTRY
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.
Description: 
37692
URI: http://hdl.handle.net/20.500.12779/4565
ISSN: 0021-9258
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