Toward an Unified Description for Thermodynamics, 검증 바카라 Kinetics, an…

"A multiscale-heterogeneous protein energy function was developed for the biophysical study of the thermodynamics, 검증 바카라 kinetics, and mutagenesis of proteins. After hybridizing an atomic force-field into a coarse-grained energy function to account for the specificity of a sequence of amino acids even with the high structural homology, we constructed an exact free energy landscape of a given protein and characterized its thermodynamics and 검증 바카라-un검증 바카라 kinetics via a Chevron plot based on solving exactly a master equation, which would enable us to pursue a mutagenesis application. Our approach was applied successfully for resolving a controversy about the 검증 바카라 mechanism of fast 검증 바카라 proteins.

Recent experiments claiming that BBL protein follows a global downhill 검증 바카라 raised an important controversy as to the 검증 바카라 mechanism of fast 검증 바카라 proteins. Under the global downhill 검증 바카라 scenario not only proteins undergo a gradual 검증 바카라, but also 검증 바카라 events along the continuous 검증 바카라 pathway could be mapped out from the equilibrium denaturation experiment. Based on the exact calculation using a free energy landscape, relaxation eigenmodes from a master equation, and Monte Carlo simulation of an extended Munoz-Eaton model that incorporates multiscale-heterogeneous pairwise-interactions between amino acids, here we show that the very nature of a two-state cooperative transition such as a bimodal distribution from an exact free energy landscape and biphasic relaxation kinetics do manifest in the thermodynamics and 검증 바카라-un검증 바카라 kinetics of BBL and peripheral subunit-binding domain (PSBD) homologue. Our results provide an unequivocal resolution to the fundamental controversy related to the global downhill 검증 바카라 scheme, whose applicability to other proteins should be critically re-examined. "