000004699 001__ 4699
000004699 005__ 20200402205616.0
000004699 0247_ $$2pmid$$apmid:18853152
000004699 0247_ $$2DOI$$a10.1007/s00249-008-0375-z
000004699 0247_ $$2WOS$$aWOS:000262671600010
000004699 037__ $$aPreJuSER-4699
000004699 041__ $$aeng
000004699 082__ $$a570
000004699 084__ $$2WoS$$aBiophysics
000004699 1001_ $$0P:(DE-HGF)0$$aFabiani, E.$$b0
000004699 245__ $$aDynamics of apo-myoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein
000004699 260__ $$aBerlin$$bSpringer$$c2009
000004699 300__ $$a237 - 244
000004699 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000004699 3367_ $$2DataCite$$aOutput Types/Journal article
000004699 3367_ $$00$$2EndNote$$aJournal Article
000004699 3367_ $$2BibTeX$$aARTICLE
000004699 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000004699 3367_ $$2DRIVER$$aarticle
000004699 440_0 $$010441$$aEuropean Biophysics Journal : with Biophysics Letters$$v38$$x0175-7571$$y2
000004699 500__ $$aThe authors acknowledge the IN13 and IRIS staffs for their support during the experiment at ILL and ISIS facilities. Thanks are due to Dr. Felix Fernandez-Alonso and Dr. Franz Demmel for helpful discussions. Technical and financial support from the ILL and ISIS facilities is gratefully acknowledged. The WAXS measurement was done under the approval of the JASRI Program Advisory Committee ( Proposal #2006A1339). M. Tehei acknowledges the ILL, the AINSE, the CNRS and the Institut de Biologie Structurale (UMR 5075) for financial support of this work.
000004699 520__ $$aChanges of molecular dynamics in the alpha-to-beta transition associated with amyloid fibril formation were explored on apomyoglobin (ApoMb) as a model system. Circular dichroism, neutron and X-ray scattering experiments were performed as a function of temperature on the protein, at different solvent conditions. A significant change in molecular dynamics was observed at the alpha-to-beta transition at about 55 degrees C, indicating a more resilient high temperature beta structure phase. A similar effect at approximately the same temperature was observed in holo-myoglobin, associated with partial unfolding and protein aggregation. A study in a wide temperature range between 20 and 360 K revealed that a dynamical transition at about 200 K for motions in the 50 ps time scale exists also for a hydrated powder of heat-denatured aggregated ApoMb.
000004699 536__ $$0G:(DE-Juel1)FUEK443$$2G:(DE-HGF)$$aProgramm Biosoft$$cN03$$x0
000004699 588__ $$aDataset connected to Web of Science, Pubmed
000004699 65320 $$2Author$$aAmyloid former
000004699 65320 $$2Author$$aProtein dynamics
000004699 65320 $$2Author$$aNeutron
000004699 65320 $$2Author$$aCircular dichroism
000004699 650_2 $$2MeSH$$aAmyloidosis: physiopathology
000004699 650_2 $$2MeSH$$aApoproteins: chemistry
000004699 650_2 $$2MeSH$$aCircular Dichroism
000004699 650_2 $$2MeSH$$aCrystallography, X-Ray
000004699 650_2 $$2MeSH$$aModels, Molecular
000004699 650_2 $$2MeSH$$aMyoglobin: chemistry
000004699 650_2 $$2MeSH$$aNeutron Diffraction
000004699 650_2 $$2MeSH$$aPharmaceutical Solutions
000004699 650_2 $$2MeSH$$aProtein Folding
000004699 650_2 $$2MeSH$$aProtein Multimerization
000004699 650_2 $$2MeSH$$aProtein Structure, Tertiary
000004699 650_2 $$2MeSH$$aTemperature
000004699 650_2 $$2MeSH$$aThermodynamics
000004699 650_7 $$00$$2NLM Chemicals$$aApoproteins
000004699 650_7 $$00$$2NLM Chemicals$$aMyoglobin
000004699 650_7 $$00$$2NLM Chemicals$$aPharmaceutical Solutions
000004699 650_7 $$00$$2NLM Chemicals$$aapomyoglobin
000004699 650_7 $$2WoSType$$aJ
000004699 7001_ $$0P:(DE-Juel1)VDB78506$$aStadler, A.M.$$b1$$uFZJ
000004699 7001_ $$0P:(DE-HGF)0$$aMadern, D.$$b2
000004699 7001_ $$0P:(DE-HGF)0$$aHirai, M.$$b3
000004699 7001_ $$0P:(DE-HGF)0$$aZaccai, G.$$b4
000004699 773__ $$0PERI:(DE-600)1398349-0$$a10.1007/s00249-008-0375-z$$gVol. 38, p. 237 - 244$$p237 - 244$$q38<237 - 244$$tEuropean biophysics journal$$v38$$x0175-7571$$y2009
000004699 8567_ $$uhttp://dx.doi.org/10.1007/s00249-008-0375-z
000004699 909CO $$ooai:juser.fz-juelich.de:4699$$pVDB
000004699 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000004699 9141_ $$y2009
000004699 9131_ $$0G:(DE-Juel1)FUEK443$$aDE-HGF$$bSchlüsseltechnologien$$kN03$$lBioSoft$$vProgramm Biosoft$$x0$$zentfällt
000004699 9201_ $$0I:(DE-Juel1)ISB-2-20090406$$d31.12.2010$$gISB$$kISB-2$$lMolekulare Biophysik$$x0
000004699 970__ $$aVDB:(DE-Juel1)111889
000004699 980__ $$aVDB
000004699 980__ $$aConvertedRecord
000004699 980__ $$ajournal
000004699 980__ $$aI:(DE-Juel1)ICS-6-20110106
000004699 980__ $$aUNRESTRICTED
000004699 981__ $$aI:(DE-Juel1)IBI-7-20200312
000004699 981__ $$aI:(DE-Juel1)ICS-6-20110106
000004699 981__ $$aI:(DE-Juel1)ISB-2-20090406