Application of calculated sedimentation ratios in the specification of models for protein dimers, trimers, tetramers and pentamers.
In the preceding paper a systematic method for delineating quaternary structures compatible with the sedimentation behaviour of oligomeric assemblies was developed. In this companion paper the approach is illustrated by its application to a number of oligomeric proteins, namely beta-lactoglobulin, aminoacyl transferase, succinic semialdehyde dehydrogenase, arginine decarboxylase, and the arthropod hemocyanins. Structures of these proteins based on comparisons of calculated and experimental sedimentation coefficients are presented and, wherever possible, compared with those obtained by other techniques. The usefulness and limitations of the method are assessed. It is concluded that the sedimentation analysis will usually yield a reasonably good representation of the mode of assembly of protein molecules in oligomeric structures if accurate experimental data are available. A high degree of resolution of structural detail is not expected and since, in addition, the sedimentation ratio method is seldom definitive to one structure, it is most valuable when used in a conformatory or eliminative way with results from techniques more specifically designed for structure determination.
Jeffrey
P D
PD
Department of Physical Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, A.C.T. 2601, Australia.
Andrwes
P R
PR