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

Martin Billeter, Werner Braun, Kurt Wüthrich

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Abstract

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 χi 1, 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.

Original languageEnglish (US)
Pages (from-to)321-346
Number of pages26
JournalJournal of Molecular Biology
Volume155
Issue number3
DOIs
StatePublished - Mar 5 1982
Externally publishedYes

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Protein Conformation
Protons
Magnetic Resonance Spectroscopy
Proteins
Amides
Amino Acid Sequence
Aromatic Amino Acids
Asparagine
Glutamine
Theoretical Models
Peptides

ASJC Scopus subject areas

  • Virology

Cite this

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title = "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",
abstract = "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 χi 1, 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.",
author = "Martin Billeter and Werner Braun and Kurt W{\"u}thrich",
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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

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 χi 1, 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 χi 1, 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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