EconPapers    
Economics at your fingertips  
 

Dynamic stability and thermodynamic characterization in an enzymatic reaction at the single molecule level

Moisés Santillán

Physica A: Statistical Mechanics and its Applications, 2011, vol. 390, issue 21, 4038-4044

Abstract: In this work we study, at the single molecular level, the thermodynamic and dynamic characteristics of an enzymatic reaction comprising a rate limiting step. We investigate how the stability of the enzyme-state stationary probability distribution, the reaction velocity, and its efficiency of energy conversion depend on the system parameters. We employ in this study a recently introduced formalism for performing a multiscale thermodynamic analysis in continuous-time discrete-state stochastic systems.

Keywords: Irreversible thermodynamics; Non-equilibrium steady state; Reaction velocity; Efficiency; Relaxation rate (search for similar items in EconPapers)
Date: 2011
References: View complete reference list from CitEc
Citations:

Downloads: (external link)
http://www.sciencedirect.com/science/article/pii/S0378437111004389
Full text for ScienceDirect subscribers only. Journal offers the option of making the article available online on Science direct for a fee of $3,000

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:390:y:2011:i:21:p:4038-4044

DOI: 10.1016/j.physa.2011.05.032

Access Statistics for this article

Physica A: Statistical Mechanics and its Applications is currently edited by K. A. Dawson, J. O. Indekeu, H.E. Stanley and C. Tsallis

More articles in Physica A: Statistical Mechanics and its Applications from Elsevier
Bibliographic data for series maintained by Catherine Liu ().

 
Page updated 2025-03-19
Handle: RePEc:eee:phsmap:v:390:y:2011:i:21:p:4038-4044