Abstract
The complexity of the physical interactions which govern macromolecules, along with natural selection processes, has driven the evolution of the subtly balanced biochemical systems seen in biology, and as part of this, protein behaviour ranging from surprising to mysterious. The balances of the complex enzymatic mixtures found in vivo enable sensitive and rapid triggering of biochemical response mechanisms, for example, while maintaining the stability and adaptability required for life. This combination of stability and subtlety is found among protein structures as well: a few amino acid types with unlimited variety in sequences; a few types of secondary structure but many globular folds; common folding scaffolds (predictable?) with hypervariability at functional segments.
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Engh, R.A., Huber, R., Bode, W. (1994). Multiple Conformations of Cystatin, Mung Bean Inhibitor, and Serpins. In: Doniach, S. (eds) Statistical Mechanics, Protein Structure, and Protein Substrate Interactions. NATO ASI Series, vol 325. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1349-4_30
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