Universität zu Köln

Sarter, Mona, Niether, Doreen, Koenig, Bernd W., Lohstroh, Wiebke, Zamponi, Michaela, Jalarvo, Niina H., Wiegand, Simone ORCID: 0000-0001-6333-1956, Fitter, Joerg ORCID: 0000-0002-4503-2079 and Stadler, Andreas M. (2020). Strong Adverse Contribution of Conformational Dynamics to Streptavidin-Biotin Binding. J. Phys. Chem. B, 124 (2). S. 324 - 336. WASHINGTON: AMER CHEMICAL SOC. ISSN 1520-5207

Full text not available from this repository.

Abstract

Molecular dynamics plays an important role for the biological function of proteins. For protein ligand interactions, changes of conformational entropy of protein and hydration layer are relevant for the binding process. Quasielastic neutron scattering (QENS) was used to investigate differences in protein dynamics and conformational entropy of ligand-bound and ligand-free streptavidin. Protein dynamics were probed both on the fast picosecond time scale using neutron time-of-flight spectroscopy and on the slower nanosecond time scale using high-resolution neutron backscattering spectroscopy. We found the internal equilibrium motions of streptavidin and the corresponding mean square displacements (MSDs) to be greatly reduced upon biotin binding. On the basis of the observed MSDs, we calculated the difference of conformational entropy Delta S-conf of the protein component between ligand-bound and ligand-free streptavidin. The rather large negative Delta S-conf value (-2 kJ mol(-1) K-1 on the nanosecond time scale) obtained for the streptavidin tetramer seems to be counterintuitive, given the exceptionally high affinity of streptavidin-biotin binding. Literature data on the total entropy change Delta S observed upon biotin binding to streptavidin, which includes contributions from both the protein and the hydration water, suggest partial compensation of the unfavorable Delta S-conf by a large positive entropy gain of the surrounding hydration layer and water molecules that are displaced during ligand binding.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Sarter, Mona UNSPECIFIED UNSPECIFIED UNSPECIFIED Niether, Doreen UNSPECIFIED UNSPECIFIED UNSPECIFIED Koenig, Bernd W. UNSPECIFIED UNSPECIFIED UNSPECIFIED Lohstroh, Wiebke UNSPECIFIED UNSPECIFIED UNSPECIFIED Zamponi, Michaela UNSPECIFIED UNSPECIFIED UNSPECIFIED Jalarvo, Niina H. UNSPECIFIED UNSPECIFIED UNSPECIFIED Wiegand, Simone UNSPECIFIED orcid.org/0000-0001-6333-1956 UNSPECIFIED Fitter, Joerg UNSPECIFIED orcid.org/0000-0002-4503-2079 UNSPECIFIED Stadler, Andreas M. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-348712
DOI:	10.1021/acs.jpcb.9b08467
Journal or Publication Title:	J. Phys. Chem. B
Volume:	124
Number:	2
Page Range:	S. 324 - 336
Date:	2020
Publisher:	AMER CHEMICAL SOC
Place of Publication:	WASHINGTON
ISSN:	1520-5207
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Physical Chemistry
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language LIGAND-BINDING; MOLECULAR RECOGNITION; NANOSECOND DYNAMICS; GLOBULAR-PROTEINS; X-RAY; ENTROPY; ASSOCIATION; ENERGETICS; SCATTERING; ENERGY Multiple languages Chemistry, Physical Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/34871