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The domains of protein S from Myxococcus xanthus: structure, stability and interactions.
Investigation of the stability and folding of natural protein S and its isolated domains found well-defined domain interactions contribute significantly to the overall stability of intact protein S. Expand
Folding and self-assembly of the domains of betaB2-crystallin from rat eye lens.
As shown by urea-induced equilibrium unfolding experiments, the isolated monomeric C-terminal domain is more stable than complete betaB2, whereas the isolated domains may be quantitatively described by the two-state model (N <==> U). Expand
Eye lens betaB2-crystallin: circular permutation does not influence the oligomerization state but enhances the conformational stability.
To the authors' knowledge this is the first circularly permuted protein which exhibits a higher stability than the corresponding wild-type protein, as judged by circular dichroism and fluorescence. Expand
Domain interactions and connecting peptides in lens crystallins.
It is concluded that the domain-interface itself rather than the connecting peptide determines the mode of domain association in crystallins, as the linker in the gamma B beta-mutant is evidently twisted to a turn similar to the one in natural gamma B-crystallin. Expand
The domains in γB-crystallin: Identical fold-different stabilities
The strongly decreased stability of the C-terminal domain at acid pH allowed a dissection of the intrinsic stabilities of the domains and their interactions in γB-crystallin. Expand
The domains in gammaB-crystallin: identical fold-different stabilities.
The strongly decreased stability of the C-terminal domain at acid pH allowed a dissection of the intrinsic stabilities of the domains and their interactions in gammaB-crystallin. Expand
Kinetic and Thermodynamic Stabilization of the βγ-Crystallin Homolog Spherulin 3a from Physarum polycephalum by Calcium Binding
Abstract Globular proteins may be stabilized, either intrinsically, at the various levels of the structural hierarchy, or extrinsically, by ligand binding. In the case of the dormant all-β proteinExpand
Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution.
The structural relationship between spherulin 3a, a myxomycete dormancy protein, and crystallins from the vertebrate eye lens is shown and represents a hypothetical ancestral gamma-crystallin precursor structure. Expand
Kinetic stabilisation of a modular protein by domain interactions
To determine the stability of the single domains and to explain the ubiquitous domain duplication, the isolated domains of protein S were constructed, finding the N‐domain is thermodynamically more stable than the C‐domain. Expand
A Zinc Cluster Transcription Factor Contributes to the Intrinsic Fluconazole Resistance of Candida auris
A possible involvement of related transcription factors in efflux pump expression and fluconazole resistance of C. auris is investigated and a transcription factor is identified that contributes to the high resistance to flu Conazole and voriconazole of two C. Aurora strains from different genetic clades, thereby providing insight into the molecular basis of drug resistance of this medically important yeast. Expand