Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3964
Title: Probing Protein-structure By Solvent Perturbation of Nmr-spectra .2. Determination of Surface and Buried Residues In Homologous Proteins
Authors: G., Esposito
A. M., Lesk
H., Molinari
A., Motta
Niccolai, Neri 
A., Pastore
Issue Date: 1993
Project: None 
Journal: BIOPOLYMERS
Abstract: 
The experimental assignment of most residues in a protein to the surface or interior is in principle possible without prior solution of a complete three-dimensional structure. The method described is based on nmr measurements that determine the amino acid composition of the surface of a protein [A. Petros, L. Mueller, and K. D. Kopple (1990) Biochemistry, Vol. 29, pp. 10041-10048; G. Esposito, A. M. Lesk, H. Molinari, A. Motta, N. Niccolai, and A. Pastore (1992) Journal of Molecular Biology, Vol. 224, pp. 659-670]. If these measurements are carried out on several homologous proteins of known sequence, it is possible to combine the results to determine, in most cases, which positions in the sequence contain exposed residues.
Description: 
47491
URI: http://hdl.handle.net/20.500.12779/3964
ISSN: 0006-3525
DOI: 10.1002/bip.360330512
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