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Title
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NMR-spectroscopic mapping of an engineered cavity in the I14A mutant of HPr from Staphylococcus carnosus using xenon.
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Authors
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C.Gröger,
A.Möglich,
M.Pons,
B.Koch,
W.Hengstenberg,
H.R.Kalbitzer,
E.Brunner.
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Ref.
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J Am Chem Soc, 2003,
125,
8726-8727.
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PubMed id
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Abstract
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The interaction between the histidine-containing phosphocarrier protein HPr and
xenon atoms in solution is studied in the present paper. Wild-type HPr as well
as the exchange mutant I14A have been studied. Specific binding of xenon into an
engineered cavity created via the exchange of amino acid residue I14 by alanine
could be shown using 1H-15N heteronuclear single-quantum coherence (HSQC)
spectroscopy. Xenon binding results in pronounced changes of the 1H and 15N
chemical shifts of amide groups close to the cavity. In addition to this
observation which allows the NMR-spectroscopic mapping of such cavities, we have
shown that the entire molecule is slightly rearranged as a result of xenon
binding. In contrast, wild-type HPr only exhibits minor chemical shift changes
due to the nonspecific interactions with the xenon atoms in solution.
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