Conformational preference of ChaK1 binding peptides: a molecular dynamics study
نویسندگان
چکیده
منابع مشابه
Conformational preference of ChaK1 binding peptides: a molecular dynamics study
TRPM7/ChaK1 is a recently discovered atypical protein kinase that has been suggested to selectively phosphorylate the substrate residues located in alpha-helices. However, the actual structure of kinase-substrate complex has not been determined experimentally and the recognition mechanism remains unknown. In this work we explored possible kinase-substrate binding modes and the likelihood of an ...
متن کاملPutative Binding Sites of Dopamine and Arachidonoyl Dopamine to Beta-lactoglobulin: A Molecular Docking and Molecular Dynamics Study
Because of participation in many aspects of human life, and due to oxidation-sensitive characteristics of dopamine (DA) and arachidonoyl dopamine (AA-DA), the necessity of biocompatible carrier to keep them against oxidation is of importance. In this work, we explored the putative binding sites of DA and AA-DA to -lactoglobulin (BLG) as potent carrier. Docking results identified the binding si...
متن کاملDisorder in Cholesterol-Binding Functionality of CRAC Peptides: A Molecular Dynamics Study
The cholesterol recognition/interaction amino acid consensus (CRAC) motif is a primary structure pattern used to identify regions that may be responsible for preferential cholesterol binding in many proteins. The leukotoxin LtxA, which is produced by a pathogenic bacterium, contains two CRAC seqences, only one of which is responsible for cholesterol binding, and the binding is required for cyto...
متن کاملConformational Fluctuations in Proteins: a Molecular Dynamics based study
excitation of native fluctuations during thermal unfolding simulations: horse heart cytochrome c, a case study. Biophys. Conformational fluctuations and electronic properties in myoglobin. A. Di Nola. Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin. Biophys. A. Di Nola. Molecular dynamics simulations of sperm whale myoglobin: effects of mutations...
متن کاملMolecular dynamics study of conformational changes in human serum albumin by binding of fatty acids.
Human serum albumin (HSA) binds with fatty acids under normal physiologic conditions. To date, there is little published information on the tertiary structure of HSA-fatty acid complex in aqueous solution. In the present study, we used molecular dynamics (MD) simulations to elucidate possible structural changes of HSA brought about by the binding of fatty acids. Both unliganded HSA and HSA-fatt...
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: PMC Biophysics
سال: 2010
ISSN: 1757-5036
DOI: 10.1186/1757-5036-3-2