Abstract
Even the most general conception of the protein molecule — which is imagined as a homopolymer with a linear memory — necessarily involves its capability of fluctuation (Lifshits, 1968; Lifshits and Grosberg, 1973). Statistical analysis indicates that the homopolymeric coil executes continuous macroscopic pulsations, and that its density is not a thermodynamically reliable magnitude. If T < T kr , a kind of coil-to-globule phase transition takes place under the effect of a sufficiently powerful compressing field.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1985 D. Reidel Publishing Company, Dordrecht, Holland
About this chapter
Cite this chapter
Käiväräinen, A.I. (1985). Conformational Mobility of Proteins. In: Käiväräinen, A.I. (eds) Solvent-Dependent Flexibility of Proteins and Principles of Their Function. Advances in Inclusion Science, vol 2. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-5197-6_3
Download citation
DOI: https://doi.org/10.1007/978-94-009-5197-6_3
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-8798-8
Online ISBN: 978-94-009-5197-6
eBook Packages: Springer Book Archive