Intrinsically Unfolded Protein
Mostrando 1-5 de 5 artigos, teses e dissertações.
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1. FEZ1 protein : little organizational structure, activities related to elements of the cytoskeleton and generation of the "flower like" phenotype / A proteina FEZ1 : pouca organização estrutural, atividades associadas a elementos do citoesqueleto e formação do fenotipo "flower like"
FEZ1 was identified first as a orthologue of C elegans UNC-76 protein, that plays functions related to neuronal development in this worm. Subsequent studies, shows FEZ1 functions in neuronal development process, cell polarization, transport mechanisms associated to kinesins and vesicular and mitochondrial transports. Other works showed that FEZ1 superexpress
Publicado em: 2009
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2. Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils
Although a diversity of proteins is known to form amyloid fibers, their common mechanisms are not clear. Here, we show that an intrinsically unfolded protein (U), represented by a disulfide-deficient variant of hen lysozyme with no tertiary structure, forms an amyloid-like fibril after prolonged incubation. Using variable pressure NMR along with sedimentatio
National Academy of Sciences.
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3. A Self-Consistent Description of the Conformational Behavior of Chemically Denatured Proteins from NMR and Small Angle Scattering
Characterization of the conformational properties of unfolded proteins is essential for understanding the mechanisms of protein folding and misfolding. This information is also fundamental to determining the relationship between flexibility and function in the highly diverse families of intrinsically disordered proteins. Here we present a self-consistent mod
The Biophysical Society.
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4. Zinc Ion-induced Domain Organization in Metallo-β-lactamases: A FLEXIBLE “ZINC ARM” FOR RAPID METAL ION TRANSFER?*
The reversible unfolding of metallo-β-lactamase from Chryseobacterium meningosepticum (BlaB) by guanidinium hydrochloride is best described by a three-state model including folded, intermediate, and unfolded states. The transformation of the folded apoenzyme into the intermediate state requires only very low denaturant concentrations, in contrast to the Zn2
American Society for Biochemistry and Molecular Biology.
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5. Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration.
Studies of numerous proteins with infrared spectroscopy have documented that unfolding is a general response of unprotected proteins to freeze-drying. Some proteins that are unfolded in the dried solid aggregate during rehydration, whereas others refold. It has been proposed for the latter case that aggregation is avoided because refolding kinetically outcom