6533b826fe1ef96bd1283dfe

RESEARCH PRODUCT

Comparison of neutron and X-ray scattering of dilute myoglobin solutions.

K. IbelH.b. Stuhrmann

subject

MaleProtein ConformationAstrophysics::High Energy Astrophysical PhenomenaNeutron scatteringInelastic scatteringOpticsStructural BiologyMethodsAnimalsScattering RadiationMolecular BiologyPhysicsNeutronsQuasielastic scatteringScatteringbusiness.industryMyoglobinX-RaysWhalesDeuteriumSmall-angle neutron scatteringComputational physicsQuasielastic neutron scatteringScattering theoryBiological small-angle scatteringbusinessMathematics

description

Experimental results obtained by neutron scattering of dilute solutions of myoglobin are compared with those obtained by X-ray scattering. X-ray scattering remains the more powerful technique at wider angles above 0.3 A−1, where neutron experiments are less accurate because of low coherent scattering probability and high incoherent background. Neutron scattering is preferable at momentum transfers below 0.2 A−1; the conditions for applying the contrast variation method for the evaluation of the three basic scattering functions, which are due to shape and internal structure, equation (3), are ideally fulfilled in this region. Furthermore, neutrons allow observation of the hydrogen-deuterium exchange within the protein.

yearjournalcountryeditionlanguage
1975-04-05Journal of molecular biology
10.1016/0022-2836(75)90131-xhttps://pubmed.ncbi.nlm.nih.gov/1171250