000205072 001__ 205072
000205072 005__ 20240619083514.0
000205072 037__ $$aFZJ-2015-05548
000205072 041__ $$aEnglish
000205072 1001_ $$0P:(DE-Juel1)130829$$aMeier, G.$$b0$$eCorresponding author
000205072 1112_ $$aECNS2015$$cZaragoza$$d2015-08-30 - 2015-09-04$$wSpain
000205072 245__ $$aStructure of the Intrinsically Disordered Protein Otholith in Solution at Different Protein and Salt Concentrations
000205072 260__ $$c2015
000205072 3367_ $$033$$2EndNote$$aConference Paper
000205072 3367_ $$2DataCite$$aOther
000205072 3367_ $$2BibTeX$$aINPROCEEDINGS
000205072 3367_ $$2DRIVER$$aconferenceObject
000205072 3367_ $$2ORCID$$aLECTURE_SPEECH
000205072 3367_ $$0PUB:(DE-HGF)6$$2PUB:(DE-HGF)$$aConference Presentation$$bconf$$mconf$$s1479484491_15473$$xOther
000205072 520__ $$aTwo members of the intrinsically disordered proteins (IDP) family (OMM-64 and STM) have been studied by means of small angle neutron scattering (SANS), dynamic light scattering (DLS) and fluorescence correlation spectroscopy (FCS). SANS curves of the proteins in D2O buffers have been measured for a range of Na+ and Ca2+ salts concentrations. The same samples have been measured using DLS in order to estimate their apparent hydrodynamic radii (Rh) and the scattering intensity in the q = 0 limit. The size of the proteins as a function of Na+ and Ca2+ concentrations had been measured in nano-molar concentrations using FCS. Fits to the SANS data suggest a coiled structure of the proteins in solution. For the first time SANS curves of proteins embedded in calcium carbonate crystals have been measured. Also a coiled structure has been found (slope = -2). Exact values of the radius of gyration (Rg) from SANS need measurements at smaller q-values.
000205072 536__ $$0G:(DE-HGF)POF3-551$$a551 - Functional Macromolecules and Complexes (POF3-551)$$cPOF3-551$$fPOF III$$x0
000205072 7001_ $$0P:(DE-HGF)0$$aBanachowicz, E.$$b1
000205072 7001_ $$0P:(DE-HGF)0$$aPoznar, M.$$b2
000205072 7001_ $$0P:(DE-HGF)0$$aPatkowski, A.$$b3
000205072 7001_ $$0P:(DE-HGF)0$$aGapinski, J.$$b4
000205072 7001_ $$0P:(DE-HGF)0$$aKohlbrecher, J.$$b5
000205072 7001_ $$0P:(DE-HGF)0$$aWilk-Kohlbrecher, A.$$b6
000205072 909CO $$ooai:juser.fz-juelich.de:205072$$pVDB
000205072 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)130829$$aForschungszentrum Jülich GmbH$$b0$$kFZJ
000205072 9131_ $$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$$x0
000205072 9141_ $$y2015
000205072 920__ $$lyes
000205072 9201_ $$0I:(DE-Juel1)ICS-3-20110106$$kICS-3$$lWeiche Materie $$x0
000205072 980__ $$aconf
000205072 980__ $$aVDB
000205072 980__ $$aI:(DE-Juel1)ICS-3-20110106
000205072 980__ $$aUNRESTRICTED