Transiently disordered tails accelerate folding of globular proteins.
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TLDR
The surprising result that an increased percentage of terminal short transiently disordered regions with enhanced flexibility (TstDREF) is associated with accelerated folding rates of globular proteins is shown.About:
This article is published in FEBS Letters.The article was published on 2017-07-01 and is currently open access. It has received 4 citations till now. The article focuses on the topics: Folding (chemistry) & Protein folding.read more
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A topological study of protein folding kinetics
Eleni Panagiotou,Kevin W. Plaxco +1 more
TL;DR: The results suggest that the global topology/geometry of the proteins shifts from right-handed to left-handed with decreasing folding rate, and that this topological change is associated with an increase in the number of more sequence-distant contacts.
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The protein folding rate and the geometry and topology of the native state
TL;DR: In this article , a small set of two-state and multi-state proteins with no knots or slipknots were analyzed and 95.4% of the analyzed proteins have non-trivial topological characteristics, as reflected by the second Vassiliev measure, and the logarithm of the experimental protein folding rate depends on both the local geometry and the topology of the protein's native state.
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On the Effects of Disordered Tails, Supertertiary Structure and Quinary Interactions on the Folding and Function of Protein Domains
Francesca Malagrinò,Valeria Pennacchietti,Daniele Santorelli,Livia Pagano,Caterina Nardella,Awa Diop,Angelo Toto,Stefano Gianni +7 more
TL;DR: It is shown that, in many cases, both the folding and function of protein domains is remarkably perturbed by the presence of these interactions, pinpointing the importance to increase the level of complexity of the experimental work and to extend the efforts to characterize protein domains in more complex contexts.
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The protein folding rate and the geometry and topology of the native state
Jason Wang,Eleni Panagiotou +1 more
TL;DR: In this article, a small set of two-state and multi-state proteins with no knots or slipknots was analyzed and it was shown that 95.4% of the analyzed proteins have non-trivial topological characteristics, as reflected by the second Vassiliev measure.
References
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The Protein Data Bank
Helen M. Berman,John D. Westbrook,Zukang Feng,Gary L. Gilliland,Talapady N. Bhat,Helge Weissig,Ilya N. Shindyalov,Philip E. Bourne +7 more
TL;DR: The goals of the PDB are described, the systems in place for data deposition and access, how to obtain further information and plans for the future development of the resource are described.
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Why are "natively unfolded" proteins unstructured under physiologic conditions?
TL;DR: Analysis of amino acid sequences, based on the normalized net charge and mean hydrophobicity, has been applied to two sets of proteins and shows that “natively unfolded” proteins are specifically localized within a unique region of charge‐hydrophobia phase space.
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IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
TL;DR: The IUPred server presents a novel algorithm for predicting such regions from amino acid sequences by estimating their total pairwise interresidue interaction energy, based on the assumption that IUP sequences do not fold due to their inability to form sufficient stabilizing inter Residue interactions.
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Contact order, transition state placement and the refolding rates of single domain proteins
TL;DR: Investigations have revealed statistically significant correlations between the average sequence separation between contacting residues in the native state and the rate and transition state placement of folding for a non-homologous set of simple, single domain proteins, indicating that proteins featuring primarily sequence-local contacts tend to fold more rapidly and exhibit less compact folding transition states than those characterized by more non-local interactions.
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Converging concepts of protein folding in vitro and in vivo
TL;DR: Recent concepts emerging from studies of protein folding in vitro and in vivo are reviewed, with a focus on how proteins navigate the complex folding energy landscape inside cells with the aid of molecular chaperones.