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PDBsum entry 1oa6
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Hydrolase inhibitor
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PDB id
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1oa6
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The solution structure of bovine pancreatic trypsin inhibitor at high pressure.
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Authors
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M.P.Williamson,
K.Akasaka,
M.Refaee.
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Ref.
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Protein Sci, 2003,
12,
1971-1979.
[DOI no: ]
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PubMed id
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Abstract
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The solution structure of bovine pancreatic trypsin inhibitor (BPTI) at a
pressure of 2 kbar is presented. The structure was calculated as a change from
an energy-minimized low-pressure structure, using (1)H chemical shifts as
restraints. The structure has changed by 0.24 A RMS, and has almost unchanged
volume. The largest changes as a result of pressure are in the loop 10-16, which
contains the active site of BPTI, and residues 38-42, which are adjacent to
buried water molecules. Hydrogen bonds are compressed by 0.029 +/- 0.117 A, with
the longer hydrogen bonds, including those to internal buried water molecules,
being compressed more. The hydrophobic core is also compressed, largely from
reduction of packing defects. The parts of the structure that have the greatest
change are close to buried water molecules, thus highlighting the importance of
water molecules as the nucleation sites for volume fluctuation of proteins in
native conditions.
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Figure 1.
Figure 1. Radial distribution functions for low- and
high-pressure BPTI structures. The family 8 results are shown as
an illustration. Distances were calculated between all pairs of
atoms (including hydrogens) and placed into 0.1 Å bins. The
distributions were weighted by dividing the number in each bin
by the square of the radius. (A) The functions for the
low-pressure structure (solid line) and the high-pressure
structure (dashed line). (B) The difference (high - low), such
that a positive peak at any distance means that there are more
atom pairs at this distance in the high-pressure structure than
there are in the low-pressure structure.
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Figure 8.
Figure 8. Relative locations of Cys51 and Phe45 in low- and
high-pressure structures. The two structures were superimposed
on the ring atoms of Phe45.
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2003,
12,
1971-1979)
copyright 2003.
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