[Size of a human serum albumin molecule in solution].
The size of a human serum albumin molecule in aqueous solution containing 150 mM NaCl was studied using small-angle neutron scattering. The molecular radius of gyration was estimated to be 27.4 +/- 0.35 A. The compact sphere should have a smaller radius of gyration, whereas the popular human serum albumin model, a "cigar" 136 A long, should correspond to a greater radius of gyration. Possible shapes of the human serum albumin molecule which are in accordance with the results obtained, are the following: an extended ellipsoid less than 110 A of length or a nonsymmetrical oblate ellipsoid with a diameter of 85 A. The oblate ellipsoid might be close to the heart"-shaped structure of the crystalline human serum albumin molecule. The size of the albumin molecule does not change significantly as pH increases to 8.9. The possibility of the dynamic coexistence of various human serum albumin conformers in solution is discussed.
Kiselev
M A
MA
Joint Institute of Nuclear Research, Dubna, 141 980 Russia.
Gryzunov
Iu A
IuA
Dobretsov
G E
GE
Komarova
M N
MN
D006801:Humans; D009502:Neutrons; D012542:Scattering, Radiation; D012709:Serum Albumin / Q000737:chemistry*; D012965:Sodium Chloride; D012996:Solutions; D014867:Water
D012709:Serum Albumin; D012996:Solutions; D014867:Water; D012965:Sodium Chloride