000835134 001__ 835134
000835134 005__ 20240619083540.0
000835134 037__ $$aFZJ-2017-05002
000835134 041__ $$aEnglish
000835134 1001_ $$0P:(DE-Juel1)131034$$aWiegand, Simone$$b0$$eCorresponding author$$ufzj
000835134 1112_ $$cGarching$$wGermany
000835134 245__ $$aWhat can we learn about complex formation by combining thermophoresis with QENS?$$f2017-07-10 - 
000835134 260__ $$c2017
000835134 3367_ $$033$$2EndNote$$aConference Paper
000835134 3367_ $$2DataCite$$aOther
000835134 3367_ $$2BibTeX$$aINPROCEEDINGS
000835134 3367_ $$2ORCID$$aLECTURE_SPEECH
000835134 3367_ $$0PUB:(DE-HGF)31$$2PUB:(DE-HGF)$$aTalk (non-conference)$$btalk$$mtalk$$s1500881767_6034$$xInvited
000835134 3367_ $$2DINI$$aOther
000835134 502__ $$cTUM
000835134 520__ $$aMolecular recognition via protein–ligand interactions is of fundamental importance to most processes occurring within living organisms. Structural fluctuations and conformational motions of proteins are essential for the binding of ligands and other interaction partners. This binding process is governed by equilibrium thermodynamics and the minimization of the free energy ΔG for the whole system. Also the thermophoresis, the diffusion in a temperature gradient, is sensitive to the complex formation. This effect has been used intensively to gain detailed information on binding dynamics, but the physicochemical processes are still unclear [1]. The strong sensitivity of proteins and other water soluble biomolecules to the temperature gradient is probably caused by a change in the hydration layer, which is influenced by subtle conformation changes induced by the binding of the ligand molecule. We want to correlate the information about the hydration layer obtained in thermophoresis experiments with changes of structural fluctuations and conformational motions measured by quasi-elastic incoherent neutron scattering (QENS) and isothermal titration calorimetry (ITC). As model system we want to study streptavidin-biotin. Streptavidin is a 58.8 kDa protein with an extremely high affinity for the ligand biotin (also known as vitamin B7 or vitamin H). The thermodiffusion is investigated  by infrared thermal diffusion forced Rayleigh scattering (IR-TDFRS) [2]. [1] M. Jerabek-Willemsen, T. André, W. Wanner, H. M. Roth, S. Duhr, P. Baaske, D. Breitsprecher, J. Mol. Struct. 2014, 1077, 101-113.[2] S. Wiegand, H. Ning, H. Kriegs, J. Phys. Chem. B 2007, 111, 14169-14174.
000835134 536__ $$0G:(DE-HGF)POF3-551$$a551 - Functional Macromolecules and Complexes (POF3-551)$$cPOF3-551$$fPOF III$$x0
000835134 909CO $$ooai:juser.fz-juelich.de:835134$$pVDB
000835134 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131034$$aForschungszentrum Jülich$$b0$$kFZJ
000835134 9131_ $$0G:(DE-HGF)POF3-551$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vFunctional Macromolecules and Complexes$$x0
000835134 9141_ $$y2017
000835134 920__ $$lyes
000835134 9201_ $$0I:(DE-Juel1)ICS-3-20110106$$kICS-3$$lWeiche Materie $$x0
000835134 980__ $$atalk
000835134 980__ $$aVDB
000835134 980__ $$aI:(DE-Juel1)ICS-3-20110106
000835134 980__ $$aUNRESTRICTED