TY - JOUR
T1 - An NMR approach to structural proteomics
AU - Yee, Adelinda
AU - Chang, Xiaoqing
AU - Pineda-Lucena, Antonio
AU - Wu, Bin
AU - Semesi, Anthony
AU - Le, Brian
AU - Ramelot, Theresa
AU - Lee, Gregory M.
AU - Bhattacharyya, Sudeepa
AU - Gutierrez, Pablo
AU - Denisov, Aleksej
AU - Lee, Chang Hun
AU - Cort, John R.
AU - Kozlov, Guennadi
AU - Liao, Jack
AU - Finak, Grzegorz
AU - Chen, Limin
AU - Wishart, David
AU - Lee, Weontae
AU - McIntosh, Lawrence P.
AU - Gehring, Kalle
AU - Kennedy, Michael A.
AU - Edwards, Aled M.
AU - Arrowsmith, Cheryl H.
PY - 2002/2/19
Y1 - 2002/2/19
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=18244366113&partnerID=8YFLogxK
U2 - 10.1073/pnas.042684599
DO - 10.1073/pnas.042684599
M3 - Article
C2 - 11854485
AN - SCOPUS:18244366113
SN - 0027-8424
VL - 99
SP - 1825
EP - 1830
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 4
ER -