Results 11 to 20 of about 41,661 (301)
Self‐recognition by an intrinsically disordered protein [PDF]
The intrinsically disordered translocation domain (T‐domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T‐domain of colicin N known to bind to the helper protein TolA in target cells also ...
Hecht O +7 more
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Intrinsic Structural Disorder in Cytoskeletal Proteins [PDF]
Cytoskeleton, the internal scaffold of the cell, displays an exceptional combination of stability and dynamics. It is composed of three major filamentous networks, microfilaments (actin filaments), intermediate filaments (neurofilaments), and microtubules.
Guha Roy, Mainak +4 more
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Intrinsic Fluorescence of Intrinsically Disordered Proteins
Resolution of the intrinsic emission properties of a protein by different fluorescence spectroscopy techniques is an invaluable tool to detect and characterize its structural architecture and conformational changes under different experimental conditions.
NEYROZ, PAOLO, CIURLI, STEFANO LUCIANO
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Databases for intrinsically disordered proteins [PDF]
Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature.
Piovesan, Damiano +3 more
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Many different intrinsically disordered proteins and proteins with intrinsically disordered regions are associated with neurodegenerative diseases. These types of proteins including amyloid-β, tau, α-synuclein, CHCHD2, CHCHD10, and G-protein coupled receptors are increasingly becoming evaluated as potential drug targets in the pharmaceutical-based ...
Orkid Coskuner-Weber +2 more
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Introducing Protein Intrinsic Disorder [PDF]
Central to this model is the notion that the correct shape of the substrate can fit into the active site of the enzyme for enabling an efficient and specific catalysis, as observed for enzymes that hydrolyze β-but not α-glycosidic bonds. 1 Throughout the 20 th century, tens of thousands of structures have been solved and deposited in the Protein Data ...
Habchi, Johnny +3 more
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Protein flexibility and intrinsic disorder [PDF]
AbstractComparisons were made among four categories of protein flexibility: (1) low‐B‐factor ordered regions, (2) high‐B‐factor ordered regions, (3) short disordered regions, and (4) long disordered regions. Amino acid compositions of the four categories were found to be significantly different from each other, with high‐B‐factor ordered and short ...
Radivojac, P. +7 more
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Intrinsically disordered proteins and biomineralization [PDF]
In vertebrates and invertebrates, biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners.
Adele L, Boskey +1 more
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Intrinsically Disordered Proteins: An Overview
Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states. Such intrinsically disordered proteins or protein segments are highly abundant across proteomes, and are involved in various effector functions.
Rakesh Trivedi +1 more
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Testing the length limit of loop grafting in a helical repeat protein
Alpha-helical repeat proteins such as consensus-designed tetratricopeptide repeats (CTPRs) are exceptionally stable molecules that are able to tolerate destabilizing sequence alterations and are therefore becoming increasingly valued as a modular ...
Juliane F. Ripka +3 more
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