this report contains our progress to date in determining the function of the d-7 lea proteins in cotton embryos. we have completely sequenced the d-7 gene and established (ital e. coli) transformants which synthesize reasonable amounts of the d-7 protein two-dimensional electrophoresis was required to assay fractions for d-7 protein during purification to homogeneity, since d-7 has no known enzymatic activity, contains no trp, and little phe or tyr, and (ital e. coli) has several proteins of similar molecular weight to d-7. purified d-7 was used to generate monospecific antibodies which are being used for determination of the cellular distribution of d-7, and also for exact quantitation of d-7 in late-stage cotton embryos computerized modelling of d-7 has shown similarities to proteins with a coiled-coil structure, but fitting d-7 to this structure resulted in a violation of the handedness rule. if the pitch of the helix is changed from 3.6 to 3.667, however, a three dimensional structure (not a coiled coil) is generated which has overall energetics of formation nearly as favorable as the traditional (alpha) helix. the driving force for the change in pitch is proposed to result from favorable energetics of dimerization. preliminary evidence indicates that d-7 does indeed dimerize in solution. future experiments will determine the exact 3d structure of d-7 and the related protein d-29, as well as test the hypothesis that d-7 and d-29 are involved in mitigating dehydration of embryos and plants through sequestering phosphate or other ions in sufficient quantity to prevent ion