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

doi:10.1006/JMBI.1999.3110

Journal ArticleDOI

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

Peter E. Wright, +1 more

- 22 Oct 1999 -

Journal of Molecular Biology

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

Daniel J. Klionsky, +2522 more

- 21 Jan 2016 -

Autophagy

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.

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Functional organization of the yeast proteome by systematic analysis of protein complexes

Anne-Claude Gavin, +37 more

- 10 Jan 2002 -

Nature

TL;DR: The analysis provides an outline of the eukaryotic proteome as a network of protein complexes at a level of organization beyond binary interactions, which contains fundamental biological information and offers the context for a more reasoned and informed approach to drug discovery.

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Intrinsically unstructured proteins and their functions.

H. Jane Dyson, +1 more

- 01 Mar 2005 -

Nature Reviews Molecular Cell Biology

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.

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Journal ArticleDOI

Why are "natively unfolded" proteins unstructured under physiologic conditions?

Vladimir N. Uversky, +3 more

- 15 Nov 2000 -

Proteins

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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Intrinsically unstructured proteins.

Peter Tompa

- 01 Oct 2002 -

Trends in Biochemical Sciences

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.

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References

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Peter O'Hare, +1 more

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Biochemistry

TL;DR: The overproduced and purified carboxy-terminal transactivation domain of Vmw65 (VP16) of herpes simplex virus and potential folding of the domain by 1H NMR indicate that the isolated acid domain has little if any alpha-helical content of any stable nature.

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Hsou-min Li, +3 more

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Proceedings of the National Academy of S...

TL;DR: It is shown here that in vitro translated precursor proteins of ferredoxin and plastocyanin are synthesized as apo forms and are assembled into their respective holo forms after being imported into isolated chloroplasts.

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Journal ArticleDOI

DNA-induced conformational changes are the basis for cooperative dimerization by the DNA binding domain of the retinoid X receptor

S. M. A. Holmbeck, +2 more

- 04 Dec 1998 -

Journal of Molecular Biology

TL;DR: In this paper, a single DNA half-site was found to induce conformational changes in the retinoid-X-receptor (RXR) binding to a direct repeat recognition element.

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High-resolution solution structure of the retinoid X receptor DNA-binding domain

S. M. A. Holmbeck, +5 more

- 14 Aug 1998 -

Journal of Molecular Biology

TL;DR: A high-resolution solution structure of the C195A RXRalpha DNA-binding domain is calculated using 1131 distance and dihedral angle constraints derived from 1H, 13C and 15N NMR spectra and reveals a perpendicularly packed, "loop-helix" fold similar to other nuclear hormone receptorDNA-binding domains and confirms the existence of theC-terminal helix, which was first observed in the low-resolution NMR structure.

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Probing Protein/Protein Interactions with Mass Spectrometry and Isotopic Labeling: Analysis of the p21/Cdk2 Complex

Richard W. Kriwacki, +3 more

- 05 Jun 1996 -

Journal of the American Chemical Society

TL;DR: Pro-tease mapping is an established method for probing the primary structure of proteins, ranging from random mutagenesis and chemical cross-linking to high-resolution structure determination.

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