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Research has been conducted on the protein folding reaction. The changes in CD2.d1 folding reaction heat capacity, entropy and enthalpy have been measured.

Kinetic studies reveal that the all-beta protein, 98-residue, N-terminal domain of rat CD2, folds via the rapid formation of an intermediate which precedes the rate-limiting formation of the folded state. This protein belongs to the immunoglobulin superfamily but does not have a disulfide bridge. The structure of this state has been probed by hydrogen-deuterium exchange studies and its thermodynamic properties have been assessed by the temperature dependence of its kinetic parameters. Results imply a high degree of native-like chain organization in the intermediate state.

Thermodynamic variables, namely entropy change and change in heat capacity, were examined in the folding reactions of the N-terminal domain of phosphoglycerate kinase and domain 1 of the T-cell adhesion protein CD2. The two proteins were found to have almost identical qualitative properties in the individual stages, namely transition state to the fully folded state, intermediate to major transition state and unfolded to intermediate state. The results suggested that consolidation of the structure happens in the I-to-F stage and that side-chain locking follows further dehydration.

A study was conducted on the intermediate state that is formed during the folding/unfolding of the cell-surface receptor protein CD2.D1. The acquisition of backbone hydrogen bonds made between sequence-local and sequence-distant segments of the chain during folding is also analyzed. The results indicate that the essential features of the Beta-sheet topology of CD2.D1 are defined early in the folding pathway.

I hate ironing; I'll do more or less anything to avoid it. I started to wonder why those shirts emerged from the clothes dryer looking like a tangled bag of [...]