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000008207 084__ $$2WoS$$aBiochemistry & Molecular Biology
000008207 084__ $$2WoS$$aBiophysics
000008207 1001_ $$0P:(DE-HGF)0$$aGaspar, A.M.$$b0
000008207 245__ $$aUsing polarization analysis to separate the coherent and incoherent scattering from protein samples
000008207 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2010
000008207 300__ $$a76 - 82
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000008207 440_0 $$0802$$aBiochimica et Biophysica Acta$$v1804$$x0006-3002$$y1
000008207 500__ $$aA. M. Gaspar acknowledges the support given by Fundacao para Ciencia e Tecnologia in the form of a post-doc grant SFRH/BDP/17571/2004. The project was further supported by a grant of the Deutsche Forschungsgemeinschaft SFB 533.
000008207 520__ $$aPolarization analysis was used to separate experimentally the coherent and spin-incoherent nuclear static scattering functions, from a representative set of samples of interest for protein studies. This method had so far limited application in the study of amorphous materials, despite the relevance of the information that it provides. It allows, for instance, the experimental determination of the structure factor of materials containing a significant amount of hydrogen atoms, avoiding the contamination of measurements by a non-negligible incoherent background. Knowledge of the relative importance of the coherent and incoherent terms at different Q-values is also a pre-requisite for the interpretation of quasielastic neutron scattering experiments, performed at instruments in which the total dynamic scattering function is measured, such as conventional time-of-flight and backscattering spectrometers. Combining data from different instruments, it was possible to cover a wide Q-range, from the small-angle region (0.006<Q<0.04 A(-1)) to the wide-angle region (up to approximately 2.35 A(-1)). Quantitative information was obtained on the fraction of coherent to spin-incoherent scattering from different protein samples: deuterated and protonated protein powders at different hydration levels and solutions of protonated proteins in D(2)O at different concentrations. The results obtained are discussed in the context of the validity of the assumptions generally made when interpreting quasielastic neutron scattering experiments performed without polarization analysis.
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000008207 65320 $$2Author$$aNeutron scattering
000008207 65320 $$2Author$$aPolarization analysis
000008207 65320 $$2Author$$aCoherent/incoherent nuclear scattering
000008207 65320 $$2Author$$aProtonated/deuterated protein
000008207 65320 $$2Author$$aStructure
000008207 65320 $$2Author$$aDynamic
000008207 650_2 $$2MeSH$$aDeuterium Oxide: chemistry
000008207 650_2 $$2MeSH$$aHemoglobins: chemistry
000008207 650_2 $$2MeSH$$aModels, Chemical
000008207 650_2 $$2MeSH$$aMyoglobin: chemistry
000008207 650_2 $$2MeSH$$aNeutron Diffraction: methods
000008207 650_2 $$2MeSH$$aPhycocyanin: chemistry
000008207 650_2 $$2MeSH$$aProteins: chemistry
000008207 650_2 $$2MeSH$$aSolutions
000008207 650_2 $$2MeSH$$aWater: chemistry
000008207 650_7 $$00$$2NLM Chemicals$$aHemoglobins
000008207 650_7 $$00$$2NLM Chemicals$$aMyoglobin
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000008207 650_7 $$07732-18-5$$2NLM Chemicals$$aWater
000008207 650_7 $$07789-20-0$$2NLM Chemicals$$aDeuterium Oxide
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