Equilibria of oligomeric proteins under high pressure - A theoretical description

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F16%3A10330478" target="_blank" >RIV/00216208:11310/16:10330478 - isvavai.cz</a>

Alternative codes found

RIV/70883521:28110/16:43875599

Result on the web

<a href="http://dx.doi.org/10.1016/j.jtbi.2016.10.001" target="_blank" >http://dx.doi.org/10.1016/j.jtbi.2016.10.001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jtbi.2016.10.001" target="_blank" >10.1016/j.jtbi.2016.10.001</a>

Result language

angličtina

Original language name

Equilibria of oligomeric proteins under high pressure - A theoretical description

Original language description

High pressure methods have become a useful tool for studying protein structure and stability. Using them, various physico-chemical processes including protein unfolding, aggregation, oligomer dissociation or enzyme activity decrease were studied on many different proteins. Oligomeric protein dissociation is a process that can perfectly utilize the potential of high-pressure techniques, as the high pressure shifts the equilibria to higher concentrations making them better observable by spectroscopic methods. This can be especially useful when the oligomeric form is highly stable at atmospheric pressure. These applications may be, however, hindered by less intensive experimental response as well as interference of the oligomerization equilibria with unfolding or aggregation of the subunits, but also by more complex theoretical description. In this study we develop mathematical models describing different kinds of oligomerization equilibria, both closed (equilibrium of monomer and the highest possible oligomer without any intermediates) and consecutive. Closed homooligomer equilibria are discussed for any oligomerization degree, while the more complex heterooligomer equilibria and the consecutive equilibria in both homo-and heterooligomers are taken into account only for dimers and trimers. In all the cases, fractions of all the relevant forms are evaluated as functions of pressure and concentration. Significant points (inflection points and extremes) of the resulting transition curves, that can be determined experimentally, are evaluated as functions of pressure and/or concentration. These functions can be further used in order to evaluate the thermodynamic parameters of the system, i.e. atmospheric-pressure equilibrium constants and volume changes of the individual steps of the oligomer-dissociation processes.

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

—

Project

<a href="/en/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Controlling structure and function of biomolecules at the molecular scale: theory meets experiment</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Theoretical Biology

ISSN

0022-5193

e-ISSN

—

Volume of the periodical

411

Issue of the periodical within the volume

21 prosince 2016

Country of publishing house

US - UNITED STATES

Number of pages

11

Pages from-to

16-26

UT code for WoS article

000389963000003

EID of the result in the Scopus database

2-s2.0-84991709186