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Part of the book series: Advances in Inclusion Science ((AIS,volume 2))

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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.

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© 1985 D. Reidel Publishing Company, Dordrecht, Holland

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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

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  • 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

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