1oa5
|
THE SOLUTION STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR AT HIGH PRESSURE
OverviewOverview
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.
About this StructureAbout this Structure
1OA5 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
The solution structure of bovine pancreatic trypsin inhibitor at high pressure., Williamson MP, Akasaka K, Refaee M, Protein Sci. 2003 Sep;12(9):1971-9. PMID:12930996
Page seeded by OCA on Tue Nov 20 22:53:11 2007