Tier-0 protein dynamics of bovine serum albumin: A kinetics and energetics study of the collective domain motions

The time-resolved confocal fluorescent thermometry coupled with a reversible two-state model were employed to characterize the thermally-induced dynamics of bovine serum albumin (BSA) on a millisecond timescale. Fluorescence intensity change of the constituent tryptophans in BSA was recorded upon a 5 degrees C temperature jump from different initial temperatures (25-42 degrees C). An apparent activation energy of 78 +/- 6 kJ mol(-1) was derived for quantifying the inter-basin conversion of the energy landscape, in terms of Tier 0 dynamics, which is plausibly associated with the collective structural alteration in the vicinity of constituent tryptophan Trp-134.

Automated summary

In this study, time-resolved confocal fluorescent thermometry coupled with a reversible two-state model was used to characterize the thermally-induced dynamics of bovine serum albumin (BSA) on a millisecond timescale. The fluorescence intensity change of constituent tryptophans in BSA was recorded after a 5 degrees C temperature jump from various initial temperatures. An apparent activation energy of 78 +/- 6 kJ mol(-1) was derived to quantify the inter-basin conversion of the energy landscape related to Tier 0 dynamics and potentially linked to collective structural alterations near constituent tryptophan Trp-134.