Dynamical properties of bovine pancreatic trypsin inhibitor from a molecular dynamics simulation at 5000 atm
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(93)81342-W/fullpdf
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2. Activation volumes for the rotational motion of interior aromatic rings in globular proteins determined by high resolution 1 H NMR at variable pressure
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4. Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres
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1. Role of water in the pressure-induced unfolding of Bovine Pancreatic Trypsin Inhibitor (BPTI) protein: A molecular dynamics study;Chemical Physics Letters;2024-04
2. Correlation between protein conformations and water structure and thermodynamics at high pressure: A molecular dynamics study of the Bovine Pancreatic Trypsin Inhibitor (BPTI) protein;The Journal of Chemical Physics;2023-03-01
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4. High-pressure protein crystallography of hen egg-white lysozyme;Acta Crystallographica Section D Biological Crystallography;2015-03-26
5. High-pressure SANS and fluorescence unfolding study of calmodulin;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2014-09
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