| Literature DB >> 11854485 |
Adelinda Yee1, Xiaoqing Chang, Antonio Pineda-Lucena, Bin Wu, Anthony Semesi, Brian Le, Theresa Ramelot, Gregory M Lee, Sudeepa Bhattacharyya, Pablo Gutierrez, Aleksej Denisov, Chang-Hun Lee, John R Cort, Guennadi Kozlov, Jack Liao, Grzegorz Finak, Limin Chen, David Wishart, Weontae Lee, Lawrence P McIntosh, Kalle Gehring, Michael A Kennedy, Aled M Edwards, Cheryl H Arrowsmith.
Abstract
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.Mesh：
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Year: 2002 PMID： 11854485 PMCID： PMC122278 DOI： 10.1073/pnas.042684599
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205