Journal Article10.1016/S0959-440X(02)00289-0
Coupling of folding and binding for unstructured proteins
H. Jane Dyson,Peter E. Wright +1 more
1.3K
TL;DR: There are now numerous examples of proteins that are unstructured or only partially structured under physiological conditions and yet are nevertheless functional.
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About: This article is published in Current Opinion in Structural Biology. The article was published on 01 Feb 2002. The article focuses on the topics: Intrinsically disordered proteins & Folding funnel.
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Citations
A novel strategy for the purification of recombinantly expressed unstructured protein domains.
TL;DR: A combined heat lysis and pre-purification procedure after expressing the disordered domains in E. coli results in the irreversible denaturation and precipitation of the majority of bacterial proteins.
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Influence of sequence changes and environment on intrinsically disordered proteins.
TL;DR: Analyzing intrinsically disordered regions in the same or similar proteins crystallized independently and studying their sensitivity to changes in protein sequence and parameters of crystallographic experiments indicates that their appearance in X-ray structures dramatically depends on changes in amino acid sequence and peculiarities of the crystallographic experiment.
Conformational dynamics of partially denatured myoglobin studied by time-resolved electrospray mass spectrometry with online hydrogen-deuterium exchange.
TL;DR: This study demonstrates the use of electrospray mass spectrometry in conjunction with rapid online mixing ("time-resolved" ESI-MS) for monitoring protein conformational dynamics under equilibrium conditions.
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Heterotrimeric G protein signaling via GIV/Girdin: Breaking the rules of engagement, space, and time
TL;DR: This work provides the most complete up‐to‐date review of the molecular mechanisms that govern the unique spatiotemporal aspects of non‐canonical G protein activation by GIV and the relevance of this new paradigm in health and disease.
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Effect of arginine loss in myelin basic protein, as occurs in its deiminated charge isoform, on mediation of actin polymerization and actin binding to a lipid membrane in vitro
TL;DR: This posttranslational modification of MBP, which occurs early in life and is increased in multiple sclerosis, attenuates the ability ofMBP to polymerize and bundle actin, and to bind it to a negatively charged membrane.
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References
MOLMOL: a program for display and analysis of macromolecular structures.
TL;DR: Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, and identification and listing of short distances between pairs of hydrogen atoms.
7.3K
A homochiral metal-organic porous material for enantioselective separation and catalysis
TL;DR: The synthesis of a homochiral metal–organic porous material that allows the enantioselective inclusion of metal complexes in its pores and catalyses a transesterification reaction in an enantiOSElective manner is reported.
3.8K
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
Peter E. Wright,H. Jane Dyson +1 more
TL;DR: 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.
3K
Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain.
Paul H. Kussie,Svetlana Gorina,Vincent Marechal,Brian Elenbaas,Jacque Moreau,Arnold J. Levine,Nikola P. Pavletich +6 more
TL;DR: The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-Residue transactivation domain peptide of p53 revealed that MDM 2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic α helix, supporting the hypothesis thatMDM2 inactivates p53 by concealing its transactivationdomain.
2.2K
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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