TY - JOUR
T1 - Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations
AU - Billeter, Martin
AU - Braun, Werner
AU - Wüthrich, Kurt
N1 - Funding Information:
Important input for the present paper came from the experimental studies carried out by Dr G. Wagner. G. Wider and Dr K. H. Lee. In particular, the fundamental ideas for the joint statistics were developed in discussions with Dr Wagner. We are also indebted to Mrs J. Richardson for stimulating discussions on various aspects of protein conformations, and thank Mrs E. H. Hunziker and Mrs E. Huber for the careful preparation of the illustrations and the manuscript. Financial support was obtained from the Schweizerischer Nationalfonds (project 3528.79) and through special grants of the Eidgeniissische Technische Hochschule (ETH) Ziirich. One of the authors (M.B.) was the recipient of a fellowship of the Schweizerische Kommission fiir Molekularbiologie. Use of the facilities at the Zentrum fiir Interaktives Rechnen of the ETH is gratefully acknowledged.
PY - 1982/3/5
Y1 - 1982/3/5
N2 - Two different, theoretical studies of intramolecular proton-proton distances in polypeptide chains are described. Firstly, the distances between amide, Cα and Cβ protons of neighbouring residues in the amino acid sequence, which correspond to the sterically allowed values for the dihedral angles φi, ψi and χi1, were computed. Secondly, the frequency with which short distances occur between amide, Cα and Cβ protons of neighbouring and distant residues in the amino acid sequence were statistically evaluated in a representative sample of globular protein crystal structures. Both approaches imply that semi-quantitative measurements of short, non-bonding proton-proton distances, e.g. by nuclear Overhauser experiments, should present a reliable and generally applicable method for sequential, individual resonance assignments in protein 1H nuclear magnetic resonance spectra. Similar calculations imply that corresponding distance measurements can be used for resonance assignments in the side-chains of the aromatic amino acid residues, asparagine and glutamine, where the complete spin systems cannot usually be identified from through-bond spin-spin coupling connectivities.
AB - Two different, theoretical studies of intramolecular proton-proton distances in polypeptide chains are described. Firstly, the distances between amide, Cα and Cβ protons of neighbouring residues in the amino acid sequence, which correspond to the sterically allowed values for the dihedral angles φi, ψi and χi1, were computed. Secondly, the frequency with which short distances occur between amide, Cα and Cβ protons of neighbouring and distant residues in the amino acid sequence were statistically evaluated in a representative sample of globular protein crystal structures. Both approaches imply that semi-quantitative measurements of short, non-bonding proton-proton distances, e.g. by nuclear Overhauser experiments, should present a reliable and generally applicable method for sequential, individual resonance assignments in protein 1H nuclear magnetic resonance spectra. Similar calculations imply that corresponding distance measurements can be used for resonance assignments in the side-chains of the aromatic amino acid residues, asparagine and glutamine, where the complete spin systems cannot usually be identified from through-bond spin-spin coupling connectivities.
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U2 - 10.1016/0022-2836(82)90008-0
DO - 10.1016/0022-2836(82)90008-0
M3 - Article
C2 - 7077676
AN - SCOPUS:0020475305
SN - 0022-2836
VL - 155
SP - 321
EP - 346
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -