Equilibrium folding intermediates of a greek key β-barrel protein

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Equilibrium folding intermediates of a Greek key beta-barrel protein.

Protein S is a calcium-binding protein comprising two Greek key beta-barrel domains. We have used NMR and optical spectroscopies to show that, in the absence of calcium, the N-terminal domain of protein S forms two equilibrium folding intermediates that are in slow exchange. The intermediates arise from differential calcium-dependent folding of subdomains which are not contiguous along the poly...

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Kinetic and equilibrium folding intermediates.

Our recent experiments on the molten globule state and other protein folding intermediates lead to following conclusions: (i) the molten globule is separated by intramolecular first-order phase transitions from the native and unfolded states and therefore is a specific thermodynamic state of protein molecules; (ii) the novel equilibrium folding intermediate (the 'pre-molten globule' state) exis...

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Kinetic and equilibrium folding intermediates

O u r recent experim ents on the m olten globule state and o ther protein folding in term ediates lead to following conclusions: (i) the m olten globule is separated by in tram olecular first-order phase transitions from the native and unfolded states and therefore is a specific therm odynam ic state of protein molecules; (ii) the novel equilibrium folding in term ediate (the ‘pre-m olten g lob...

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Membrane Defects Accelerate Outer Membrane β-Barrel Protein Folding

Outer membrane β-barrel proteins spontaneously fold into lipid bilayers with rates of folding that are strongly influenced by the physical properties of the membrane. We show that folding is accelerated when the bilayer is at the phase transition temperature, because of the coexistence of lipid phase domains and the high degree of defects present at domain boundaries. These results are consiste...

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Characterizing protein folding intermediates.

To determine the pathway by which a protein folds up, it is necessary to characterize the structures of folding intermediates and also to place these intermediates in the correct order on the kinetic pathway of folding. Noncovalent folding reactions are fast: typically they occur in seconds or less for small single-domain proteins. On the other hand, hours are required to obtain detailed struct...

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ژورنال

عنوان ژورنال: Journal of Molecular Biology

سال: 1998

ISSN: 0022-2836

DOI: 10.1006/jmbi.1997.1563