Dynamics of polyglutamic acids in α-helical and coil states. Comparison with dynamics of some globular proteins. Rayleigh scattering of Mössbauer radiation (RSMR) data

Yu F. Krupyanskii, I. V. Kurinov, S. A. Kuznetsov, G. V. Eshenko, F. Parak

Research output: Contribution to journalReview articlepeer-review

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Abstract

The classical model system, poly-L-glutamic acid (poly-Glu), was investigated in a disordered coil state (at pH = 7.0) and in helix state (at pH = 2.0) by the RSMR technique. By considering that the coil state of poly-Glu models unfolded (random coil) state and α-helix state models the fluctuating secondary structure (during consequent folding of protein), a comparative analysis of the dynamical properties of poly-Glu in different states with the dynamical properties of different proteins in the native state (α-helical myoglobin and HSA, partially β-sheet lysozyme) and in intermediate (molten globule) state (α-lactalbumin) was performed. This comparison brings some unpredicted results: native α-helical proteins behave close to random coil, native partially β-sheet proteins behave close to fluctuating secondary structure (α-helix) and the dynamic behaviour of molten-globule state (partially β-sheet α-lactalbumin) is not different from the behaviour of lysozyme and much more rigid than that of native α-helical proteins.

Original languageEnglish
Pages (from-to)365-369
Number of pages5
JournalIl Nuovo Cimento D
Volume18
Issue number2-3
DOIs
StatePublished - 1996

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