Heat-induced reversible and irreversible alterations in the structure of phaseolus vulgaris thylakoid proteins

Chloroplast thylakoids isolated from bean (Phaseolus vulgaris L.) leaves have been used as a model system to identify heat-induced changes in membrane protein structure. Susceptibility of SDS gel electrophoresis bands to trypsin digestion was used as an assay for altered structure of proteins comprising the bands. Both reversible and irreversible alternations in membrane protein structure have been observed as a result of exposure to 35 or 45°C for varying time periods.