New measurements on ultrasound absorption of aqueous solutions of the three globular proteins, bovine hemoglobin, horse heart myoglobin, and bovine serum albumin, at 20 degrees C are reported for the frequency range below 1.2 MHz and, in the case of hemoglobin and bovine serum albumin, to a limited extent for the range 2-30 MHz. The effect of protein conformation has been investigated by use of a range of denaturants and by change of pH. A much more detailed description of protein interactions emerges from the low-frequency studies than was possible hitherto. Specific absorption processes for myoglobin and bovine serum albumin peak in the neighborhood of pH 4.2. The process for myoglobin has a relaxation frequency between 1 and 2.6 MHz, while for bovine serum albumin the frequency is as low as 70 kHz. Both processes can be related to conformational changes in the molecules. In the case of hemoglobin, an absorption process with a relaxation frequency of 600 kHz is found that can be attributed to the dissociation equilibrium of the quaternary structure of the molecule and can be considerably enhanced by denaturants or pH change from neutral to acid conditions. Measurements at frequencies down to 200 kHz have also permitted a more thorough investigation of proton-transfer reactions at carboxyl and amino groups in these proteins and of the effect of pH on these reactions.