Journal ArticleDOI
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
Peter E. Wright,H. Jane Dyson +1 more
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.About:
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.read more
Citations
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Atomistic Details of the Disordered States of KID and pKID. Implications in Coupled Binding and Folding
Debabani Ganguly,Jianhan Chen +1 more
TL;DR: The results suggest that an implicit solvent-based modeling framework, despite various existing limitations, might be feasible for accurate atomistic simulation of small IDPs in general and generalized Born (GB) implicit solvent, combined with replica exchange (REX) might offer an optimal balance between accuracy and efficiency.
Journal ArticleDOI
Role of the Biomolecular Energy Gap in Protein Design, Structure, and Evolution
Sarel J. Fleishman,David Baker +1 more
TL;DR: This Perspective explores the implications of this energy gap for computing the structures of naturally occurring biopolymers, designing proteins with new structures and functions, and optimally integrating experiment and computation in these endeavors.
Journal ArticleDOI
β-Lactoglobulin Molten Globule Induced by High Pressure
TL;DR: HHP treatments induce ‚-LG into hydrophobic molten globule structures that remain stable for at least 3 months, suggesting an increase in accessible aromatic hydrophobicity and a decrease in aliphatic hydrophOBicity.
Journal ArticleDOI
A free-energy landscape for coupled folding and binding of an intrinsically disordered protein in explicit solvent from detailed all-atom computations.
TL;DR: Both population-shift and induced-fit mechanisms work cooperatively in the coupled folding and binding of neural restrictive silencer factor, and the diverse structural adaptability of NRSF may be related to the hub properties of the IDP.
Journal ArticleDOI
Reconciling observations of sequence-specific conformational propensities with the generic polymeric behavior of denatured proteins.
TL;DR: This work attempts to solve the "reconciliation problem" by simulating conformational ensembles accessible to peptides and proteins in the excluded-volume limit, and results are consistent with experimental observations of sequence-specific conformational preferences in short peptide sequences and the scaling behavior of polymeric quantities for denatured proteins.
References
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The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
TL;DR: It is demonstrated that p300/CBP acetylates nucleosomes in concert with PCAF, a novel class of acetyltransferases in that it does not have the conserved motif found among various other acetyl transferases.
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The Structural Basis of Estrogen Receptor/Coactivator Recognition and the Antagonism of This Interaction by Tamoxifen
Andrew K. Shiau,Danielle Barstad,Paula M. Loria,Lin Cheng,Peter J. Kushner,David A. Agard,Geoffrey L. Greene +6 more
TL;DR: Crystal structures of the human estrogen receptor alpha (hER alpha) ligand-binding domain (LBD) and the OHT-LBD complex reveal the two distinct mechanisms by which structural features of OHT promote this "autoinhibitory" helix 12 conformation.
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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
TL;DR: The X-ray crystal structure of a core synaptic fusion complex containing syntaxin-1A, synaptobrevin-II and SNAP-25B reveals a highly twisted and parallel four-helix bundle that differs from the bundles described for the haemagglutinin and HIV/SIV gp41 membrane-fusion proteins.
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Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.
Keh-Ming Pan,Michael J. Baldwin,J Nguyen,María Gasset,Ana Serban,Darlene Groth,Ingrid Mehlhorn,Ziwei Huang,Robert J. Fletterick,Fred E. Cohen +9 more
TL;DR: It is argued that the conversion of alpha-helices into beta-sheets underlies the formation of PrPSc, and it is likely that this conformational transition is a fundamental event in the propagation of prions.
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A signature motif in transcriptional co-activators mediates binding to nuclear receptors.
TL;DR: It is proposed that the LXXLL motif is a signature sequence that facilitates the interaction of different proteins with nuclear receptors, and is thus a defining feature of a new family of nuclear proteins.