Thermodynamics and Molecular Simulation Analysis of Hydrophobic Substrate Recognition by Aminotransferases
نویسندگان
چکیده
منابع مشابه
Thermodynamics and molecular simulation analysis of hydrophobic substrate recognition by aminotransferases.
Aromatic amino acid aminotransferase (AroAT) and aspartate aminotransferase (AspAT) are known as dual-substrate enzymes, which can bind acidic and hydrophobic substrates in the same pocket (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63). In order to elucidate the mechanism of hydrophobic substrate recognition, kinetic a...
متن کاملa comparative move analysis of the introduction sections of ma theses by iranian and native post-graduate students
since esp received universal attention to smooth the path for academic studies and productions, a great deal of research and studies have been directed towards this area. swales’ (1990) model of ra introduction move analysis has served a pioneering role of guiding many relevant studies and has proven to be productive in terms of helpful guidelines that are the outcome of voluminous productions ...
15 صفحه اولIntroduction to Molecular Simulation and Statistical Thermodynamics
• Please report errors, corrections, and other suggestions to t.j.h.vlugt (at) tudelft.nl • Disclaimer: Neither the publisher nor any of the authors guarantee that this book is free from error. Neither do they accept responsibility for any loss or damage (direct or conse-quential) that results from its use.
متن کاملInvestigation of Melting by Molecular Dynamics Simulation
The melting of a 64 ion microcrystal of KCI was studied by means of a molecular dynamics computer simulation. We used a central pair interaction with an inverse power law repulsion. The thermodynamics, kinetic and structural properties such as melting temperature, latent heat, mean square displacement, diffusion constant, radial distribution function and bond angle distribution are calculated. ...
متن کاملMolecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin.
Prefoldin (PFD) is a jellyfish-shaped molecular chaperone that has been proposed to play a general role in de novo protein folding in archaea and is known to assist the biogenesis of actins, tubulins, and potentially other proteins in eukaryotes. Using point mutants, chimeras, and intradomain swap variants, we show that the six coiled-coil tentacles of archaeal PFD act in concert to bind and st...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1998
ISSN: 0021-9258
DOI: 10.1074/jbc.273.29.18353