GroEL-GroES-Mediated protein folding

Article Abstract:

The transition from the binding-active to the folding-active state of the GroEL machine is regarded as a single structural shift involving the coordinated movement of the apical domains coupled to ATP and GroES binding. The regain of fluorescence of GFP upon spontaneous refolding from denaturant is a single exponential process, but restoration of fluorescence assissted by GroEL-GroES-ATP, both in ensemble and single molecule studies, show a delay of about 3 seconds.

Fluorescence spectroscopy

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Bona fide predictions of protein secondary structure using transparent analyses of multiple sequence alignments

Article Abstract:

Bona fide prediction in the analysis of protein secondary structures may more accurately produce theoretical protein conformations. Bona fide predictions are presented before the results are tested experimentally, rather than constructed to prove a structural model already known. Predictions may be based on analysis of homologous proteins and consideration of molecular evolutionary constraints.

Methods, Proteins, Protein research, Amino acid sequence, Amino acid sequencing, Protein conformation

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Probing protein folding and conformational transitions with fluorescence

Article Abstract:

Classical and novel examples of a variety of fluorescence experimental approaches are presented to the study of protein folding. The reason fluorescence is widely applied to studies of protein folding and protein conformational dynamics stems from three fundamental properties of this technique.

Fluorescence microscopy, Conformational analysis

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