Structure-function models

King RS, Sharma V, Pedersen LC, Kakuta Y, Negishi M, Duffel MW. Structure-function modeling of the interactions of the A-alkyl-A-hydroxyanilines with rat hepatic aryl sulfotransferase IV. Chem Res Toxicol 2000 13 1251-8. 

The fundamental driving force behind the remarkable elastic properties of the elastin polymer is believed to be entropic, where stretching decreases the entropy of the system and elastic recoil is driven by a spontaneous return to maximum entropy. The precise molecular basis for elasticity has not been fully elucidated and a number of models exist. Two main categories of structure-function models have been proposed those in which elastin is considered to be isotropic and devoid of structure, and those which consider elastin to be anisotropic with regions of order (Vrhovski and Weiss, 1998). 

Lock, M. A., R. R. Wallace, J. W. Costerton, R. M. Ventullo, and S. E. Charlton. 1984. River epilithon Toward a structural-functional model. OIKOS 42 10-22. 

In addition to the predictable variation in rate among the three codon positions there is also variation in the rate of evolution from codon to codon. Thomas and Beckenbach (1989) described spatial heterogeneity in the distributions of mutations from four mitochondrial protein genes in fishes. Spatial heterogeneity in the mitochondrial cytochrome b genes of a wide variety of vertebrates fits predictions based on previous structure/function models (Kocher et al. 1989, Irwin et al. in press). 

Majumdar A, Sarkar S (2011) Bioinorganic chemistry of molybdenum and tungsten enzymes a structural-functional modeling approach. Coord Chtan Rev 255 1039-1054. doi 10.1016/j.ccr.2010.11.027... 

Toxicol., 13, 1251 (2000). Structure-Function Modeling of the Interactions of the N-alkyl-N-Hydroxyanilines with Rat Hepatic Aryl Sulfotransferase IV. 

Fig. 1. Structure-function model of Chlorella assimilatoiy NADH-nitrate reductase. Features of the model include four identical subunits with two diiferent binding domains and the FAD/ NADH and heme/molybdenum domains connected by a protease-sensitive hinge region. Solid arrows indicate physiological electron transfer reactions, and dashed arrows indicate electron transfer to or from artificial acceptors or donors (partial reactions). [Reproduced with permission from Solomonson et al. (1986).]...

Fig. 2. Structure-function model of spinach assimilatory NADH nitrate reductase. Native enzyme consists of two subunits, each comprising three separate domains Mo, molybdenum domain, 75 kDa Cyt-b, cytochrome bi domain, 14 kDa and FAD, FAD domain, 28 kDa, connected by the protease-sensitive hinge regions. [Reproduced with permission from Kubo et al. (1988).]...

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