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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.
Highlights
Interactions of proteins with other molecules can be ascribed to their surface features
We have shown that these “hot spots” of the protein surface can be mapped by a surface survey based on paramagnetic perturbation of conventional NMR spectra [7, 8]
Despite the high percentage of hydrated surface that is expected for proteins from static observations [22], the NMR data indicate that only a small number of water molecules are statically close enough to protons of BPTI and tendamistat to affect their resonances
Summary
1D, one-dimensional; 2D, two-dimensional; BPTI, bovine pancreatic trypsin inhibitor; ePHOGSY, enhanced protein hydration observed through gradient spectroscopy; NOE, nuclear Overhauser effect; ROE, rotating frame Overhauser effect; TEMPOL, 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl; TOCSY, total correlation spectroscopy.
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