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Dec 8 – 10, 2020 Online only
Online event
Europe/Berlin timezone

Failure of the Zimm model: Thermal unfolding of Ribonuclease A

Dec 10, 2020, 4:00 PM
Online event

Online event

Talk DN: Life Science/ Biology DN2020: Life Science/ Biology


Ralf Biehl (Forschungszentrum Jülich)


Disordered regions as found in intrinsically disordered proteins (IDP) or during protein folding define response time to stimuli and protein folding times. Neutron Spinecho Spectroscopy is a powerful tool to access directly collective motions of the unfolded chain to observe conformational relaxations. During thermal unfolding of native Ribonuclease A we examine structure and dynamics of the disordered state within a two-state transition model using polymer models including internal friction. The presence of 4 disulfide bonds alters the disordered configuration to a more compact configuration compared to a Gaussian chain that is defined by the additional links. The dynamics of the disordered chain is described by ZIMM dynamics with internal friction between neighboring amino acids. The mode structure is not changed by the additional links, but relaxation times are dominated by mode independent internal friction. Internal friction relaxation times show an Arrhenius like behavior. The dominating internal friction suppresses the characteristics of the ZIMM dynamics and suggest that the characteristic motions correspond to elastic overdamped modes similar to motions observed for folded proteins.

Primary author

Ralf Biehl (Forschungszentrum Jülich)


Jennifer Fischer (Forschungszentrum Jülich) Aurel Radulescu (Forschungszentrum Jülich GmbH, Jülich Centre for Neutron Science at MLZ) Peter Falus (Institut Laue-Langevin) Bernd Hofmann (Forschungszentrum Jülich) Dieter Richter (Forschungszentrum Jülich JCNS)

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