Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

Kurt Wüthrich; Gerhard Wider; Gerhard Wagner; Werner Braun

doi:10.1016/0022-2836(82)90007-9

Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

Kurt Wüthrich
, Gerhard Wider
, Gerhard Wagner
, Werner Braun

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

558 Scopus citations

Abstract

A general scheme is proposed for the determination of spatial protein structures by proton nuclear magnetic resonance. The scheme relies on experimental observation by two-dimensional nuclear magnetic resonance techniques of complete throughbond and through-space proton-proton connectivity maps. These are used to obtain sequential resonance assignments for the individual residues in the amino acid sequence and to characterize the spatial polypeptide structure by a tight network of semi-quantitative, intramolecular distance constraints.

Original language	English (US)
Pages (from-to)	311-319
Number of pages	9
Journal	Journal of Molecular Biology
Volume	155
Issue number	3
DOIs	https://doi.org/10.1016/0022-2836(82)90007-9
State	Published - Mar 5 1982
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/0022-2836(82)90007-9

Cite this

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title = "Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance",

abstract = "A general scheme is proposed for the determination of spatial protein structures by proton nuclear magnetic resonance. The scheme relies on experimental observation by two-dimensional nuclear magnetic resonance techniques of complete throughbond and through-space proton-proton connectivity maps. These are used to obtain sequential resonance assignments for the individual residues in the amino acid sequence and to characterize the spatial polypeptide structure by a tight network of semi-quantitative, intramolecular distance constraints.",

author = "Kurt W{\"u}thrich and Gerhard Wider and Gerhard Wagner and Werner Braun",

note = "Funding Information: The development of two-dimensional n.m.r. techniques for studies of biopolymers. which havtx a crucial role in the realization of the presently outlined scheme for protein structure dt\%ermination, is a joint project with Professor R. R. Ernst and is financed by a special grant of the Eidgenijssische Technische Hochschule. Ziirirh. We thank Professor Ernst for continued advice on all aspects of two-dimensional n.m.r. Financial support by the Schweizerischrr Nationalfonds (project 3528.79) is grat,efully acknowledged.",

year = "1982",

month = mar,

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doi = "10.1016/0022-2836(82)90007-9",

language = "English (US)",

volume = "155",

pages = "311--319",

journal = "Journal of Molecular Biology",

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TY - JOUR

T1 - Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

AU - Wüthrich, Kurt

AU - Wider, Gerhard

AU - Wagner, Gerhard

AU - Braun, Werner

N1 - Funding Information: The development of two-dimensional n.m.r. techniques for studies of biopolymers. which havtx a crucial role in the realization of the presently outlined scheme for protein structure dt%ermination, is a joint project with Professor R. R. Ernst and is financed by a special grant of the Eidgenijssische Technische Hochschule. Ziirirh. We thank Professor Ernst for continued advice on all aspects of two-dimensional n.m.r. Financial support by the Schweizerischrr Nationalfonds (project 3528.79) is grat,efully acknowledged.

PY - 1982/3/5

Y1 - 1982/3/5

N2 - A general scheme is proposed for the determination of spatial protein structures by proton nuclear magnetic resonance. The scheme relies on experimental observation by two-dimensional nuclear magnetic resonance techniques of complete throughbond and through-space proton-proton connectivity maps. These are used to obtain sequential resonance assignments for the individual residues in the amino acid sequence and to characterize the spatial polypeptide structure by a tight network of semi-quantitative, intramolecular distance constraints.

AB - A general scheme is proposed for the determination of spatial protein structures by proton nuclear magnetic resonance. The scheme relies on experimental observation by two-dimensional nuclear magnetic resonance techniques of complete throughbond and through-space proton-proton connectivity maps. These are used to obtain sequential resonance assignments for the individual residues in the amino acid sequence and to characterize the spatial polypeptide structure by a tight network of semi-quantitative, intramolecular distance constraints.

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DO - 10.1016/0022-2836(82)90007-9

M3 - Article

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AN - SCOPUS:0020475314

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VL - 155

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 3

ER -

Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

Abstract

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