Abstract
Absorption coefficient and propagation speeds for aqueous solutions of globular proteins were measured at pH 7 and 290°K. Concentrations were approximately 100 mg/ml. Proteins measured were lysozyme, γ‐globulin, myoglobin, hemoglobin, egg albumin, β‐lactoglobulin, bovine serum albumin, and bacitracin. Specific absorption and propagation speed did not correlate with molecular weight, fraction of α‐helix content, or n‐mer structure. In addition, fibrous muscle protein paramyosin, and its subunit, PPC‐1, were measured in α‐helical and random coil state. The conformation change was produced with 6M quanidine hydrochloride. The ratio of α‐helix state absorption to random coil state absorption was approximately two for PPC‐I and six for paramyosin. [Work supported by NIGMS.]
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