Using antibodies to perturb the coordination sphere of a transition metal complex

Article Abstract:

Antibodies can utilize part of their binding energy to stabilize a compressed, high energy state molecular structure, thereby influencing the coordination sphere of a given metallic complex to modify its physicochemical properties. Antibodies against a organosilicon can also bind to structurally similar Cu(I) complex. But in the process the antibody slightly compresses the Cu(I) complex to a size closer to that of organosilicon compound. Such mechanisms may be at work in the metalloenzymes to modulate the coordination sphere of a transition metal complex.

Research, Binding sites (Biochemistry), Active sites (Biochemistry), Metalloenzymes

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Characterization of a functionally important mobile domain of GroES

Article Abstract:

GroES has a very mobile and accessible polypeptide loop that may permit simultaneous binding to seven GroEL subunits at GroES-specific sites. This may coordinate GroEL's conformational changes to release substrates. The loop's mobility and accessibility are lost upon binding to GroEL. The mobility of GroES's binding sites may let them accommodate substrate-specific distortions in GroEL's tetradecamer.

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Folding dynamics and mechanism of beta-hairpin formation

Article Abstract:

Alpha-helix formation has been studied extensively in synthetic and natural peptides. However beta structures have not been studied experimentally. A simple statistical mechanical model has been developed to give a structural explanation for the folding of a beta-hairpin which occurs in 6 mus, slower than the rate of alpha-helix formation.

Observations, Protein folding

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