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

doi:10.1002/bip.360330512

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

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

9 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 language	English (US)
Pages (from-to)	839-846
Number of pages	8
Journal	Biopolymers
Volume	33
Issue number	5
DOIs	https://doi.org/10.1002/bip.360330512
State	Published - May 1993

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Biomaterials
Organic Chemistry

Access to Document

10.1002/bip.360330512

Cite this

@article{7cd160d8f5ab48f889bcb3472683174c,

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

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. {\textcopyright} 1993 John Wiley & Sons, Inc.",

author = "Gennaro Esposito and Lesk, {Arthur M.} and Henriette Molinari and Andrea Motta and Neri Niccolai and Annalisa Pastore",

year = "1993",

month = may,

doi = "10.1002/bip.360330512",

language = "English (US)",

volume = "33",

pages = "839--846",

journal = "Biopolymers",

issn = "0006-3525",

publisher = "John Wiley and Sons Inc.",

number = "5",

}

TY - JOUR

T1 - Probing protein structure by solvent perturbation of nmr spectra. II. Determination of surface and buried residues in homologous proteins

AU - Esposito, Gennaro

AU - Lesk, Arthur M.

AU - Molinari, Henriette

AU - Motta, Andrea

AU - Niccolai, Neri

AU - Pastore, Annalisa

PY - 1993/5

Y1 - 1993/5

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0027594495&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027594495&partnerID=8YFLogxK

U2 - 10.1002/bip.360330512

DO - 10.1002/bip.360330512

M3 - Article

C2 - 8343579

AN - SCOPUS:0027594495

SN - 0006-3525

VL - 33

SP - 839

EP - 846

JO - Biopolymers

JF - Biopolymers

IS - 5

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this