Entropic elastic processes in protein mechanisms. II. Simple (passive) and coupled (active) development of elastic forces.
The first part of this review on entropic elastic processes in protein mechanisms (Urry, 1988) demonstrated with the polypentapeptide of elastin (Val1-Pro2-Gly3-Val4-Gly5)n that elastic structure develops as the result of an inverse temperature transition and that entropic elasticity is due to internal chain dynamics in a regular nonrandom structure. This demonstration is contrary to the pervasive perspective of entropic protein elasticity of the past three decades wherein a network of random chains has been considered the necessary structural consequence of the occurrence of dominantly entropic elastomeric force. That this is not the case provides a new opportunity for understanding the occurrence and role of entropic elastic processes in protein mechanisms. Entropic elastic processes are considered in two classes: passive and active. The development of elastomeric force on deformation is class I (passive) and the development of elastomeric force as the result of a chemical process shifting the temperature of a transition is class II (active). Examples of class I are elastin, the elastic filament of muscle, elastic force changes in enzyme catalysis resulting from binding processes and resulting in the straining of a scissile bond, and in the turning on and off of channels due to changes in transmembrane potential. Demonstration of the consequences of elastomeric force developing as the result of an inverse temperature transition are seen in elastin, where elastic recoil is lost on oxidation, i.e., on decreasing the hydrophobicity of the chain and shifting the temperature for the development of elastomeric force to temperatures greater than physiological. This is relevant in general to loss of elasticity on aging and more specifically to the development of pulmonary emphysema. Since random chain networks are not the products of inverse temperature transitions and the temperature at which an inverse temperature transition occurs depends on the hydrophobicity of the polypeptide chain, it now becomes possible to consider chemical processes for turning elastomeric force on and off by reversibly changing the hydrophobicity of the polypeptide chain. This is herein called mechanochemical coupling of the first kind; this is the chemical modulation of the temperature for the transition from a less-ordered less elastic state to a more-ordered more elastic state. In the usual considerations to date, development of elastomeric force is the result of a standard transition from a more-ordered less elastic state to a less-ordered more elastic state.(ABSTRACT TRUNCATED AT 400 WORDS)
Urry
D W
DW
Laboratory of Molecular Biophysics, University of Alabama, Birmingham 35294.
D000595:Amino Acid Sequence; D000818:Animals; D002465:Cell Movement; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003285:Contractile Proteins / Q000502:physiology*; D004548:Elasticity; D004549:Elastin / Q000502:physiology*; D005260:Female; D006900:Hydroxylation; D007743:Labor, Obstetric / Q000502:physiology; D051379:Mice; D008969:Molecular Sequence Data; D009119:Muscle Contraction; D011247:Pregnancy; D013816:Thermodynamics
D003285:Contractile Proteins; D004549:Elastin