Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28510109
&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215
Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28510109
.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Biophys+Rev
2013 ; 5
(3
): 283-293
Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
A new theoretical approach to biological self-assembly
#MMPMID28510109
Kinoshita M
Biophys Rev
2013[Sep]; 5
(3
): 283-293
PMID28510109
show ga
Upon biological self-assembly, the number of accessible translational
configurations of water in the system increases considerably, leading to a large
gain in water entropy. It is important to calculate the solvation entropy of a
biomolecule with a prescribed structure by accounting for the change in
water-water correlations caused by solute insertion. Modeling water as a
dielectric continuum is not capable of capturing the physical essence of the
water entropy effect. As a reliable tool, we propose a hybrid of the
angle-dependent integral equation theory combined with a multipolar water model
and a morphometric approach. Using our methods wherein the water entropy effect
is treated as the key factor, we can elucidate a variety of processes such as
protein folding, cold, pressure, and heat denaturating of a protein, molecular
recognition, ordered association of proteins such as amyloid fibril formation,
and functioning of ATP-driven proteins.