The circular dichroism spectra for proteins in situ in catecholamine secretory vesicles (chromaffin granules) is presented together with an analysis of protein conformation and turbidity effects on the spectra. The calculational analysis has resolved scattering and absorption effects in the turbid suspension spectra using a coated-sphere scattering model which allows for different materials in its shell and core. The intrinsic conformation of the proteins in situ was estimated by an iterative procedure with various trial protein conformations, for the chromaffin granules both intact and after release of their contents. The resulting average secondary structures (within about 10%) are: (25% a helix, 15% ,6 structure) for the membrane proteins and (15% a helix, 5% # structure) for the soluble contents. The protein conformation did not change with osmotic release of the granule's contents. Consequently, if chromogranins are involved in a catecholamine storage complex, this is not reflected in any detectable change in their average secondary structure.Circular dichroism (CD) and optical rotatory dispersion (ORD) have proven very useful in monitoring protein and nucleic-acid conformations in solution. While the solution work has laid important groundwork for the structural interpretation of the spectra, it is the study of biopolymers in situ in functioning biological complexes that is of ultimate interest for elucidation of cellular processes. In the last few years a beginning has been made in this direction, primarily for turbid suspensions of biological membranes (1). The membrane CD and ORD spectra contain characteristic distortions in the shape and magnitude of the spectral bands, and these were experimentally shown to be caused by the scattering properties and particulate nature of the membrane suspension (1-4). Similar results were found for turbid suspensions of hemoglobin within erythrocytes (1) and for polypeptide aggregates (3). Thus, in order to interpret the spectra of such turbid suspensions, the scattering contributions had to be resolved. A theoretical analysis of the circular polarization dependence of scattered light followed (5) and formed the basis for a calculational method of analyzing distorted spectra (6). Numerical computations using this approach have appeared (7,8)