Protein conformational dynamics in the mechanism of HIV-1 protease catalysis - Wikidata - awgldk - TriplyDB

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

http://www.wikidata.org/entity/Q27676129

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Protein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structure Small Molecule Regulation of Protein Conformation by Binding in the Flap of HIV Protease Enzyme dynamics from NMR spectroscopy The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics Exposing Hidden Alternative Backbone Conformations in X-ray Crystallography Using qFit NMR studies of the dynamics of nitrophorin 2 bound to nitric oxide.Expanding the chemical toolbox for the synthesis of large and uniquely modified proteins.An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.Coupling between catalytic loop motions and enzyme global dynamics Conformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solution Modulation of HIV protease flexibility by the T80N mutation Ionization state of the catalytic dyad Asp25/25' in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis.Functional dichotomy in the 16S rRNA (m1A1408) methyltransferase family and control of catalytic activity via a novel tryptophan mediated loop reorganization Comparison of design strategies for α-helix backbone modification in a protein tertiary fold.Spin labeling and Double Electron-Electron Resonance (DEER) to Deconstruct Conformational Ensembles of HIV Protease.Long-Range Electrostatics-Induced Two-Proton Transfer Captured by Neutron Crystallography in an Enzyme Catalytic Site.Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.Pushing the Boundaries of Chemical Protein Synthesis: The Case of Ubiquitin Chains and Polyubiquitinated Peptides and Proteins.Dynamic and Electrostatic Effects on the Reaction Catalyzed by HIV-1 Protease.Inherent dynamics within the Crimean-Congo Hemorrhagic fever virus protease are localized to the same region as substrate interactions.Room Temperature Neutron Crystallography of Drug Resistant HIV-1 Protease Uncovers Limitations of X-ray Structural Analysis at 100 K.Expanding the scope of N → S acyl transfer in native peptide sequences.A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In Vitro Prediction of HIV-1 protease/inhibitor affinity using RosettaLigand.Binding of the CYK-4 subunit of the centralspindlin complex induces a large scale conformational change in the kinesin subunit.Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease."The molecule's the thing:" the promise of molecular modeling and dynamic simulations in aiding the prioritization and interpretation of genomic testing results.Effects of PRE and POST therapy drug-pressure selected mutations on HIV-1 protease conformational sampling.Inhibitor-induced conformational shifts and ligand-exchange dynamics for HIV-1 protease measured by pulsed EPR and NMR spectroscopy.A molecular engineering toolbox for the structural biologist.Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies.

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P2860

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

http://www.wikidata.org/entity/Q27676129

description

2011 nî lūn-bûn

@nan

2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

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Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

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Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

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type

label

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

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Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

@en

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

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prefLabel

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

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Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

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Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

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PNAS.1111202108

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

@en

P2093

Donald Hamelberg

http://www.w3.org/2001/XMLSchema#string

Eduardo Perozo

http://www.w3.org/2001/XMLSchema#string

H Raghuraman

http://www.w3.org/2001/XMLSchema#string

Marco Tonelli

http://www.w3.org/2001/XMLSchema#string

Stephen B H Kent

http://www.w3.org/2001/XMLSchema#string

Vladimir Yu Torbeev

http://www.w3.org/2001/XMLSchema#string

William M Westler

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P2860

Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action

HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs

Convergent chemical synthesis and crystal structure of a 203 amino acid "covalent dimer" HIV-1 protease enzyme molecule

Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site

X-ray snapshot of HIV-1 protease in action: observation of tetrahedral intermediate and short ionic hydrogen bond SIHB with catalytic aspartate

Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease

Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution

Cyclic HIV protease inhibitors: synthesis, conformational analysis, P2/P2' structure-activity relationship, and molecular recognition of cyclic ureas

The structure and function of the aspartic proteinases

Synthesis of proteins by native chemical ligation

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10.1073/PNAS.1111202108

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108

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2011-12-27T00:00:00Z

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51868928

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22158985

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3248522

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