000206042 001__ 206042
000206042 005__ 20210407180043.0
000206042 037__ $$aPUBDB-2015-00575
000206042 041__ $$aEnglish
000206042 1001_ $$0P:(DE-H253)PIP1019012$$aAvinery, Ram$$b0$$eCorresponding Author$$gmale
000206042 245__ $$aForces underlying the conformational selection of myelin basic protein$$f2012-01-01 - 2014-01-01
000206042 260__ $$aTel-Aviv$$c2014
000206042 300__ $$a-
000206042 3367_ $$2DataCite$$aOutput Types/Supervised Student Publication
000206042 3367_ $$02$$2EndNote$$aThesis
000206042 3367_ $$2BibTeX$$aMASTERSTHESIS
000206042 3367_ $$2DRIVER$$amasterThesis
000206042 3367_ $$0PUB:(DE-HGF)19$$2PUB:(DE-HGF)$$aMaster Thesis$$bmaster$$mmaster$$s1477407217_712
000206042 3367_ $$2ORCID$$aSUPERVISED_STUDENT_PUBLICATION
000206042 500__ $$aNo full text available.
000206042 502__ $$aTel-Aviv University, Masterarbeit, 2014$$bMS$$cTel-Aviv University$$d2014
000206042 520__ $$aMyelin Basic Protein (MBP) has important biological role in stabilizing and compacting the myelin sheath. Previous evidence suggest that MBP adopts a compact structure when adsorbed to negatively charged membrane and gains flexibility and expands in solution. This inherent flexibility in solution, unlike most proteins, is termed intrinsic disorder. Being highly disordered, MBP adopts a wide variety of conformations simultaneously in solution. Small angle x-ray scattering and analysis using ensemble modelling are used to quantify the conformatioal diversity under varying pH and salt conditions.MBP is a polyampholyte, having both positively and negatively charged monomers with a high excess of positive charge. At pH 7.4 the mean radius of gyration (R_g) of MBP decreases with increasing salts, with a local minimum encountered around 100mM followed by re-swelling and then re-compaction. At pH 10 MBP displays a size minimum near 100mM yet no re-compaction is observed up to 500mM salt concentration. MBP in pH 4 displays R_g trend highly similar to pH 7.4, though always with slightly larger R_g as expected with its increased net charge. Underlying forces are discussed through free energy estimates calculated using polymer physics derivations.MBP’s size minimum at 100mM salt concentration is not entirely consistent with simplistic polyampholyte view, and more likely secondary structure changes are involved. Calculations indicate that salt concentration strongly affects secondary structure selection of MBP by modulating an interplay between electrostatic interaction and polymer chain entropy. The results imply a strategy for designing structural stabilization upon adsorption to a surface.
000206042 536__ $$0G:(DE-H253)POF2-P12-20130405$$aPETRA Beamline P12 (POF2-54G14)$$cPOF2-54G14$$fPOF II$$x0
000206042 650_7 $$0V:(DE-588b)4276536-5$$2GND$$aUnveröffentlichte Hochschulschrift$$xMasterarbeit
000206042 693__ $$0EXP:(DE-H253)P-P12-20150101$$1EXP:(DE-H253)PETRAIII-20150101$$6EXP:(DE-H253)P-P12-20150101$$aPETRA III$$fPETRA Beamline P12$$x0
000206042 7001_ $$0P:(DE-H253)PIP1019036$$aBeck-Barkai, Roy$$b1
000206042 773__ $$y2014
000206042 8564_ $$uhttp://www6.tau.ac.il/beck/
000206042 909CO $$ooai:bib-pubdb1.desy.de:206042$$pVDB
000206042 9101_ $$0I:(DE-HGF)0$$6P:(DE-H253)PIP1019012$$aExternes Institut$$b0$$k>Extern
000206042 9101_ $$0I:(DE-HGF)0$$6P:(DE-H253)PIP1019036$$aExternes Institut$$b1$$k>Extern
000206042 9132_ $$0G:(DE-HGF)POF3-621$$1G:(DE-HGF)POF3-620$$2G:(DE-HGF)POF3-600$$9G:(DE-HGF)POF3-6215$$aDE-HGF$$bForschungsbereich Materie$$lVon Materie zu Materialien und Leben$$vIn-house research on the structure, dynamics and function of matter$$x0
000206042 9131_ $$0G:(DE-HGF)POF2-54G14$$1G:(DE-HGF)POF2-540$$2G:(DE-HGF)POF2-500$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$9G:(DE-H253)POF2-P12-20130405$$aDE-H253$$bStruktur der Materie$$lForschung mit Photonen, Neutronen, Ionen$$vPETRA III$$x0
000206042 920__ $$lno
000206042 9201_ $$0I:(DE-H253)EMBL-User-20120814$$kEMBL-User$$lEMBL-User$$x0
000206042 980__ $$amaster
000206042 980__ $$aVDB
000206042 980__ $$aI:(DE-H253)EMBL-User-20120814
000206042 980__ $$aUNRESTRICTED