Abstract
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 °C temperature jump from different initial temperatures (25–42 °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.
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