Published June 15, 2011 | Version v1
Journal article

Controlling protein crystal growth rate by means of temperature

  • 1. Institute of Mathematics and Physics, University of Technology and Life Sciences, PL-85796 Bydgoszcz (Poland)
  • 2. Departament de Fisica Fonamental, University of Barcelona, Av. Diagonal 647, E-08028 Barcelona (Spain)

Description

We have proposed a model to analyze the growth kinetics of lysozyme crystals/aggregates under non-isothermal conditions. The model was formulated through an analysis of the entropy production of the growth process which was obtained by taking into account the explicit dependence of the free energy on the temperature. We found that the growth process is coupled with temperature variations, resulting in a novel Soret-type effect. We identified the surface entropy of the crystal/aggregate as a decisive ingredient controlling the behavior of the average growth rate as a function of temperature. The behavior of the Gibbs free energy as a function of temperature is also analyzed. The agreement between theory and experiments is very good in the range of temperatures considered.

Availability note (English)

Available from http://dx.doi.org/10.1088/0953-8984/23/23/235101

Additional details

Identifiers

DOI
10.1088/0953-8984/23/23/235101;
PII
S0953-8984(11)77391-X;

Publishing Information

Journal Title
Journal of Physics. Condensed Matter
Journal Volume
23
Journal Issue
23
Journal Page Range
[7 p.]
ISSN
0953-8984
CODEN
JCOMEL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
43007427
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
CRYSTAL GROWTH; CRYSTALS; ENTROPY; FREE ENERGY; FREE ENTHALPY; LYSOZYME; SIMULATION; SURFACES; TEMPERATURE DEPENDENCE
Descriptors DEC
ENERGY; ENZYMES; GLYCOSYL HYDROLASES; HYDROLASES; O-GLYCOSYL HYDROLASES; ORGANIC COMPOUNDS; PHYSICAL PROPERTIES; PROTEINS; THERMODYNAMIC PROPERTIES