A hybrid NMR/SAXS-based approach for discriminating oligomeric protein interfaces using Rosetta.
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ABSTRACT:
SUBMITTER: Rossi P
PROVIDER: S-EPMC5061451 | biostudies-literature | 2015 Feb
REPOSITORIES: biostudies-literature
Publications
A hybrid NMR/SAXS-based approach for discriminating oligomeric protein interfaces using Rosetta.
Rossi Paolo P Shi Lei L Liu Gaohua G Barbieri Christopher M CM Lee Hsiau-Wei HW Grant Thomas D TD Luft Joseph R JR Xiao Rong R Acton Thomas B TB Snell Edward H EH Montelione Gaetano T GT Baker David D Lange Oliver F OF Sgourakis Nikolaos G NG
Proteins 20141219 2
Oligomeric proteins are important targets for structure determination in solution. While in most cases the fold of individual subunits can be determined experimentally, or predicted by homology-based methods, protein-protein interfaces are challenging to determine de novo using conventional NMR structure determination protocols. Here we focus on a member of the bet-V1 superfamily, Aha1 from Colwellia psychrerythraea. This family displays a broad range of crystallographic interfaces none of which ...[more]
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