An NMR Approach to Structural Proteomics

The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms w...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2002-02, Vol.99 (4), p.1825-1830
Main Authors: Yee, Adelinda, Chang, Xiaoqing, Pineda-Lucena, Antonio, Wu, Bin, Semesi, Anthony, Le, Brian, Ramelot, Theresa, Lee, Gregory M., Bhattacharyya, Sudeepa, Gutierrez, Pablo, Denisov, Aleksej, Lee, Chang-Hun, Cort, John R., Kozlov, Guennadi, Liao, Jack, Finak, Grzegorz, Chen, Limin, Wishart, David, Lee, Weontae, McIntosh, Lawrence P., Gehring, Kalle, Kennedy, Michael A., Edwards, Aled M., Arrowsmith, Cheryl H.
Format: Article
Language:English
Subjects:
Amino acids
Bacterial Proteins - chemistry
Biochemistry
Biological Sciences
Cogeneration
Cogs
Crystallography
Databases as Topic
Escherichia coli - metabolism
Genomics
Magnetic Resonance Spectroscopy - methods
Models, Molecular
NMR
Nuclear magnetic resonance
Open Reading Frames
Proteins
Proteins - chemistry
Proteomics
Research facilities
Software
Species Specificity
Structural homology
X ray spectroscopy
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Summary:The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.042684599