期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 71, 期 3, 页码 1432-1440出版社
WILEY-BLACKWELL
DOI: 10.1002/prot.21832
关键词
pressure; chemical shift; protein G; compression; structural change
资金
- Biotechnology and Biological Sciences Research Council [BB/D521230/1] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/D521230/1] Funding Source: Medline
The solution structure of the GB1 domain of protein G at a pressure of 2 kbar is presented. The structure was calculated as a change from an energy-minimised low-pressure structure using H-1 chemical shifts. Two separate changes can be characterised: a compression/distortion, which is linear with pressure; and a stabilisation of an alternative folded state. On application of pressure, linear chemical shift changes reveal that the backbone structure changes by about 0.2 angstrom root mean square, and is compressed by about 1% overall. The a-helix compresses, particularly at the C-terminal end, and moves toward the beta-sheet, while the P-sheet is twisted, with the corners closest to the at-helix curling up towards it. The largest changes in structure are along the second beta-strand, which becomes more twisted. This strand is where the protein binds to IgG. Curved chemical shift changes with pressure indicate that high pressure also populates an alternative structure with a distortion towards the C-terminal end of the helix, which is likely to be caused by insertion of a water molecule.
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