NMR studies of protein surface accessibility.
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.
Niccolai
N
N
Biomolecular Structure Research Center and Department of Molecular Biology, University of Siena, I-53100 Siena, Italy.
Ciutti
A
A
Spiga
O
O
Scarselli
M
M
Bernini
A
A
Bracci
L
L
Di Maro
D
D
Dalvit
C
C
Molinari
H
H
Esposito
G
G
Temussi
P A
PA
D007611:Aprotinin / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*
D010455:Peptides; D007611:Aprotinin; C030526:tendamistate