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Medientyp: E-Artikel Titel: Pressure‐induced changes in the solution structure of the GB1 domain of protein G Beteiligte: Wilton, David J.; Tunnicliffe, Richard B.; Kamatari, Yuji O.; Akasaka, Kazuyuki; Williamson, Mike P. Erschienen: Wiley, 2008 Erschienen in: Proteins: Structure, Function, and Bioinformatics Sprache: Englisch DOI: 10.1002/prot.21832 ISSN: 0887-3585; 1097-0134 Entstehung: Anmerkungen: Beschreibung: <jats:title>Abstract</jats:title><jats:p>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 <jats:sup>1</jats:sup>H 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 Å root mean square, and is compressed by about 1% overall. The α‐helix compresses, particularly at the C‐terminal end, and moves toward the β‐sheet, while the β‐sheet is twisted, with the corners closest to the α‐helix curling up towards it. The largest changes in structure are along the second β‐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. Proteins 2008. © 2007 Wiley‐Liss, Inc.</jats:p>