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"Domain" Coil-Globule Transition in Homopolymers
Abstract
The temperature-induced coil-globule transition has been studied in dilute aqueous solutions (with 200 mg/L SDS) for different fractions of poly(N-isopropylacrylamide) (PNIPAM) and poly(N-isopropylmethacrylamide) (PNIPMAM) using scanning microcalorimetry, diffusion, and size-exclusion chromatography (FPLC). It has been shown that both these polymers undergo a coil-globule transition upon temperature increase. This transition is accompanied by cooperative heat absorption and a decrease of heat capacity, which makes it similar to the cold denaturation of globular proteins. The globule-coil transition is an "all-or-none" process only for the fraction with the lowest molecular weight (~10x10^3), while fractions of larger molecular weights behave as if they consist of quasi-independent cooperative units, the "domains". The number of "domains" in a macromolecule is proportional to the molecular weight of the polymer. This suggests that the "domain" character of cooperative transitions in large proteins does not, in principle, need evolutionary-selected amino acid sequences but can occur even in homopolymers.
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Cited by
Xia, Y., Yin, X., Burke, N. A. D., & Stöver, H. D. H. (2005) · Macromolecules · doi:10.1021/ma050261z · Cited by 503
The pH-responsive behaviour of poly(acrylic acid) in aqueous solution is dependent on molar mass
Swift, T., Swanson, L., Geoghegan, M., & Rimmer, S. (2016) · Soft Matter · doi:10.1039/c5sm02693h · Cited by 455
Ganachaud, F., Monteiro, M. J., Gilbert, R. G., Dourges, M.-A., Thang, S. H., & Rizzardo, E. (2000) · Macromolecules · doi:10.1021/ma0003102 · Cited by 306
Metadata
- Authors
- Tiktopulo, E. I., Uversky, V. N., Lushchik, V. B., Klenin, S. I., Bychkova, V. E., & Ptitsyn, O. B.
- Venue
- Macromolecules
- Publisher
- American Chemical Society (ACS)
- Published
- 1995-10
- Volume
- 28
- Issue
- 22
- Pages
- 7519-7524
- ISSN
- 0024-9297 (ISSN-L)
- 1520-5835
- OpenAlex
- W2030505484
- Cited by
- 283
- References
- 0
- FWCI
- 1.18
- Type
- journal article
- Language
- en
- Open access
- closed
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