» Articles » PMID: 12914911

The Effects of Tubulin Denaturation on the Characterization of Its Polymerization Behavior

Overview
Journal Biophys Chem
Specialty Biochemistry
Date 2003 Aug 14
PMID 12914911
Citations 10
Authors
Affiliations
Soon will be listed here.
Abstract

We report here upon a simulation study examining the effect of a dynamic mode of tubulin denaturation upon the kinetic and thermodynamic characterisation of the polymer formed for two idealized models of a tubulin polymerization reaction: (i) an irreversibly polymerizing system; and (ii) a reversibly polymerizing system. The effects of each denaturation mode upon the two model systems behavior are highlighted by interpretation of the data in terms of the classical Oosawa reversible condensation polymerization model. We reveal here findings which suggest that the measurement strategy in concert with Tubulin's instability over the time course of the experiment may bias the results obtained so as to make an irreversible system's behavior conform to the equilibrium model or alternatively distort the results obtained from a truly reversible system to produce values of the critical concentration quite seriously in error. It was also found that Tubulin denaturation may seriously distort parameter estimates gained from a kinetic characterization of the system (e.g. nucleus size and growth rate constant).

Citing Articles

 "Meet the Editors Series": a profile of Damien Hall.

Hall D Biophys Rev. 2024; 15(6):1883-1896.

PMID: 38192343 PMC: 10771549. DOI: 10.1007/s12551-023-01176-0.


MIL-CELL: a tool for multi-scale simulation of yeast replication and prion transmission.

Hall D Eur Biophys J. 2023; 52(8):673-704.

PMID: 37670150 PMC: 10682183. DOI: 10.1007/s00249-023-01679-4.


A simple method for modeling amyloid kinetics featuring position biased fiber breakage.

Hall D Biophys Physicobiol. 2020; 17:30-35.

PMID: 33110736 PMC: 7550252. DOI: 10.2142/biophysico.BSJ-2020003.


On the nature of the optimal form of the holdase-type chaperone stress response.

Hall D FEBS Lett. 2019; 594(1):43-66.

PMID: 31432502 PMC: 6961976. DOI: 10.1002/1873-3468.13580.


Ionic liquids and protein folding-old tricks for new solvents.

Wakayama R, Uchiyama S, Hall D Biophys Rev. 2019; 11(2):209-225.

PMID: 30888574 PMC: 6441443. DOI: 10.1007/s12551-019-00509-2.