## Abstract Internal and rigidβbody motions of bovine pancreatic trypsin inhibitor (BPTI) and of water molecules surrounding the BPTI are studied in a vicinity of an energy minimum using a normal mode analysis proposed as the independent molecule model. Water's rigidβbody motion is predominant in c
Protein Dynamics Tightly Connected to the Dynamics of Surrounding and Internal Water Molecules
β Scribed by Volkhard Helms
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 436 KB
- Volume
- 8
- Category
- Article
- ISSN
- 1439-4235
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β¦ Synopsis
Abstract
Proteins are key components of biological cells. For example, enzymes catalyze biochemical reactions, membrane transporters are responsible for uptake and release of critical and superfluous components from the cell environment, and structural proteins are responsible for the stability of the cell wall and cytoskeleton. Many of the diverse protein functions involve dynamic transitions ranging from small local atomic displacements up to large allosteric conformational changes. In any conformation, proteins are in contact with the universal solvent medium of cells, water. Water not only surrounds proteins but is often an integral part of proteins and also is involved in key mechanistic steps. This Minireview discusses recent experimental and theoretical results on the role of water for protein dynamics and function.
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Heat capacity has played a prominent role in relating macroscopic and microscopic properties of small molecules and crystals. However, its diagnostic power can also be used for macromolecules such as proteins. It is shown in the present study that the macroscopically observed protein heat capacity p
The effect of progessive hydration up to 60% by weight of Hz0 and D20 on the proton relasation of polycrystalline achymotrypsin and lysozyme has been examined. The dynamical behaviour of the protein molecules was not affected by hydration. The dynamics of the water molecules was characterized. and t
A molecular dynamics simulation of the operator binding domain of the lambda repressor protein has been carried out. The protein was embedded in explicit waters, Na Ψ and CL Ψ ions. The Amber 4.1 computer package and the Cornell et al. Force field were used for energy-minimization and molecular dyna