Controlling protein crystal growth rate by means of temperature
Creators
- 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/10.1088/0953-8984/23/23/235101Additional 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