Evidence for a rapid structural change in TMV-A-protein near neutrality

Titration of TMV-A-protein from pH 8 to 7 (20°C) or raising the temperature from 4° to 20°C (pH 7) produces, within a few minutes, a reversible change in the aromatic region of the CD-spectrum, before any extensive aggregation has taken place. This spectral change is solely a matter of the conditions of the solution and not of the history of the protein. There is no further CD-change during the slow aggregation process. Thus there must be some proton-uptake within the A-protein. The results are discussed with regard to the different interpretations of the role of A-protein or double-disc in the elongation-step of TMV-“in vitro” -self-assembly.