Probing protein structure by solvent perturbation of nmr spectra. II. Determination of surface and buried residues in homologous proteins

Gennaro Esposito, Arthur M. Lesk, Henriette Molinari, Andrea Motta, Neri Niccolai, Annalisa Pastore

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8 Scopus citations

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. © 1993 John Wiley & Sons, Inc.

Original languageEnglish (US)
Pages (from-to)839-846
Number of pages8
JournalBiopolymers
Volume33
Issue number5
DOIs
StatePublished - May 1993

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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