The entropy associated with the multiplicity of structural states occupied by an ensemble of protein molecules.
The extreme structural complexity of protein molecules has been evident from the very beginning of structural studies at atomic resolution by crystallography, NMR spectroscopy, and, more recently, electron microscopy. In parallel with the subsequent explosion of structural biology were smaller efforts at unraveling the nature of internal dynamics of folded protein molecules. Fundamental theoretical considerations suggested the potential for considerable residual entropy of protein molecules, which will be expressed as fluctuations between different structural states up to and including the globally unfolded state (Cooper 1976; Welch et al. 1982). Thus internal motion is intimately connected to the internal entropy of proteins and has served to shine light on this fundamental component of protein thermodynamics. The internal...
- Wand AJ, Sharp KA (2018) Measuring entropy in molecular recognition by proteins. Annu Rev Biophys 41: in pressGoogle Scholar