Automated analysis of NMR assignments and structures for proteins

Hunter Nb Moseley; Gaetano T. Montelione

doi:10.1016/S0959-440X(99)00019-6

Automated analysis of NMR assignments and structures for proteins

Hunter Nb Moseley, Gaetano T. Montelione

Molecular and Cellular Biochemistry

Research output: Contribution to journal › Review article › peer-review

170 Scopus citations

Abstract

Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and three-dimensional structures for proteins of 50 to 200 amino acids.

Original language	English
Pages (from-to)	635-642
Number of pages	8
Journal	Current Opinion in Structural Biology
Volume	9
Issue number	5
DOIs	https://doi.org/10.1016/S0959-440X(99)00019-6
State	Published - Oct 1 1999

Bibliographical note

Funding Information:
We thank Roberto Tejero and Yuanpeng Huang for useful discussions and Rebecca Watson for her expert assistance in scientific editing. The authors’ work on automated analysis is supported by grants from the National Institutes of Health (GM-47014), the National Science Foundation (MCB-9407569 and MCB-9357526) and by a New Jersey Commission on Science and Technology Research Excellence Award.

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/S0959-440X(99)00019-6

Cite this

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title = "Automated analysis of NMR assignments and structures for proteins",

abstract = "Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and three-dimensional structures for proteins of 50 to 200 amino acids.",

author = "Moseley, {Hunter Nb} and Montelione, {Gaetano T.}",

note = "Funding Information: We thank Roberto Tejero and Yuanpeng Huang for useful discussions and Rebecca Watson for her expert assistance in scientific editing. The authors{\textquoteright} work on automated analysis is supported by grants from the National Institutes of Health (GM-47014), the National Science Foundation (MCB-9407569 and MCB-9357526) and by a New Jersey Commission on Science and Technology Research Excellence Award. ",

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AU - Montelione, Gaetano T.

N1 - Funding Information: We thank Roberto Tejero and Yuanpeng Huang for useful discussions and Rebecca Watson for her expert assistance in scientific editing. The authors’ work on automated analysis is supported by grants from the National Institutes of Health (GM-47014), the National Science Foundation (MCB-9407569 and MCB-9357526) and by a New Jersey Commission on Science and Technology Research Excellence Award.

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N2 - Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and three-dimensional structures for proteins of 50 to 200 amino acids.

AB - Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and three-dimensional structures for proteins of 50 to 200 amino acids.

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Automated analysis of NMR assignments and structures for proteins

Abstract

Bibliographical note

ASJC Scopus subject areas

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