ABSTRACT
Enzyme kinetics dominated the field of biochemical kinetics primarily because the inherent amplification property of catalytic reactions aided the quantification of product formation in the steady state. The challenge in calculating the protein structure from sequence arises from the fine balance of forces that stabilize the native state over the huge number of nonnative ones. A number of serious diseases arise when a normally functional protein misfolds into an alternate structure, which then acts as a template to propagate misfolding of other molecules and ultimately forms amyloid aggregates. Protein folding is a challenging problem to study experimentally because of the enormous number of potential intermediate states and parallel pathways that could be involved. Motor proteins are involved with chemical–mechanical energy transduction. The term "molecular motor" has been applied more generally to macromolecules that are accompanied by a large directional motion of one component relative to another, such as polymerases that move on a nucleic acid track during replication.
