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Journal ArticleDOI

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.

Peter E. Wright, +1 more
- 22 Oct 1999 - 
- Vol. 293, Iss: 2, pp 321-331
TLDR
Many proteins that lack intrinsic globular structure under physiological conditions have now been recognized, and it appears likely that their rapid turnover, aided by their unstructured nature in the unbound state, provides a level of control that allows rapid and accurate responses of the cell to changing environmental conditions.
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This article is published in Journal of Molecular Biology.The article was published on 1999-10-22. It has received 2804 citations till now. The article focuses on the topics: Protein structure function & Intrinsically disordered proteins.

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Citations
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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

Intrinsically unstructured proteins and their functions.

TL;DR: Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold, whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.
Journal ArticleDOI

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.
Journal ArticleDOI

Intrinsically unstructured proteins.

TL;DR: In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where proteins can be comprehensively classified on the basis of structure and function.
References
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Journal ArticleDOI

Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA.

TL;DR: The results indicate that the GCN4 basic region is significantly unfolded at 25 °C and that its folded, α-helical conformation is stabilized by binding to DNA.
Journal ArticleDOI

Solution Structure of a Bovine Immunodeficiency Virus Tat-TAR Peptide-RNA Complex

TL;DR: The Tat protein of bovine immunodeficiency virus binds to its target RNA, TAR, and activates transcription, and the solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy.
Proceedings Article

Protein disorder and the evolution of molecular recognition: theory, predictions and observations.

TL;DR: The role of disorder-to-order transitions in protein binding has been investigated in this paper, where it is shown that these transitions enable alternative packing interactions between side chains to accommodate the different binding targets.
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