Differential cross-sections for neutrons scattered by normal human hemoglobin have been determined over the range of concentrations from 2 to approximately 35 weight percent. Data are compared with structure factors calculated from models of monodisperse hard spheres interacting through a screened Coulomb potential. Good agreement is noted when the volume fraction eta is adjusted during multivariate fitting of data, but the fitted value of eta is always lower than expected from the known Hb concentration of the samples. Calculations of cross-sections for polydisperse scatterers suggest that the samples may contain oligomers of the fundamental tetrameric Hb molecule
AbstractThe cytoplasm of red blood cells is congested with the oxygen storage protein hemoglobin occ...
In addition to the chemical nature of the surface, the dimensions of the confining host exert a sign...
The conformations of gas-phase ions of hemoglobin, and its dimer and monomer subunits have been stud...
Differential cross-sections for neutrons scattered by normal human hemoglobin have been determined o...
Small angle neutron scattering (SANS) was used to investigate interaction forces between hemoglobin ...
By using a combination of experimental neutron scattering techniques, it is possible to obtain a sta...
We present neutron scattering measurements on the dynamics of haemoglobin (Hb) in human red blood ce...
Neutron diffraction can provide very precise stereochemical information about hydrogen bonds and oth...
AbstractSmall-angle neutron scattering (SANS) is used to probe the solution structure of two protein...
Neutron scattering has significant benefits for examining the structure of complex samples. Cold (sl...
In this study non-invasive neutron scattering techniques are used on soft condensed matter, probing ...
Measurements of the mutual diffusion coefficients (D) of the liganded human hemoglobins (Hb) oxy-HbA...
The technique of small angle neutron scattering has been used to determine the molecular shape, the ...
In addition to the chemical nature of the surface, the dimensions of the confining host exert a sign...
Small angle neutron scattering (SANS) was performed on suspensions of actively metabolising human er...
AbstractThe cytoplasm of red blood cells is congested with the oxygen storage protein hemoglobin occ...
In addition to the chemical nature of the surface, the dimensions of the confining host exert a sign...
The conformations of gas-phase ions of hemoglobin, and its dimer and monomer subunits have been stud...
Differential cross-sections for neutrons scattered by normal human hemoglobin have been determined o...
Small angle neutron scattering (SANS) was used to investigate interaction forces between hemoglobin ...
By using a combination of experimental neutron scattering techniques, it is possible to obtain a sta...
We present neutron scattering measurements on the dynamics of haemoglobin (Hb) in human red blood ce...
Neutron diffraction can provide very precise stereochemical information about hydrogen bonds and oth...
AbstractSmall-angle neutron scattering (SANS) is used to probe the solution structure of two protein...
Neutron scattering has significant benefits for examining the structure of complex samples. Cold (sl...
In this study non-invasive neutron scattering techniques are used on soft condensed matter, probing ...
Measurements of the mutual diffusion coefficients (D) of the liganded human hemoglobins (Hb) oxy-HbA...
The technique of small angle neutron scattering has been used to determine the molecular shape, the ...
In addition to the chemical nature of the surface, the dimensions of the confining host exert a sign...
Small angle neutron scattering (SANS) was performed on suspensions of actively metabolising human er...
AbstractThe cytoplasm of red blood cells is congested with the oxygen storage protein hemoglobin occ...
In addition to the chemical nature of the surface, the dimensions of the confining host exert a sign...
The conformations of gas-phase ions of hemoglobin, and its dimer and monomer subunits have been stud...