Probing protein structure by solvent perturbation of NMR spectra. II. Determination of surface and buried residues in homologous proteins.
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.
Esposito
G
G
Istituto di Biologia, Facoltà di Medicina, Università di Udine, Italy.
Lesk
A M
AM
Molinari
H
H
Motta
A
A
Niccolai
N
N
Pastore
A
A
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D012996:Solutions / Q000737:chemistry
D011506:Proteins; D012996:Solutions