Proteins are dynamic over a broad range of timescales and these conformational fluctuations play critical roles in various biological processes. The amplitudes and the timescales of motion that characterize the fluctuations of a protein under a given set of conditions can be understood in terms of an energy landscape that describes the energetic relationship between all possible protein conformations. The monograph is devoted to the structure-function-folding paradigm of a dimeric motor protein (Dynein Light Chain Protein - DLC8) . The document presents the overview of various biophysical...