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 techniques and extensively report diverse Nuclear Magnetic Resonance (NMR) spectroscopy approaches that are essential in unraveling the protein energetics and dynamics. In worldwide literature, this is one of the report of this kind and author made a sincere attempt to fulfill this demand by selecting the number of topics and orienting them into sub-sections. This detailed study will be highly useful to the biophysicists, biochemists, spectroscopists, structural biologists and advanced students. On the basis of his panoptic research this comprehensive and convincing documentation is presented.