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Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

http://www.wikidata.org/entity/Q28070759

about

Human EGF-derived direct and reverse short linear motifs: conformational dynamics insight into the receptor-binding residues.A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions.Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.Recent advances in automated protein design and its future challenges.Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins

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P2860

Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

http://www.wikidata.org/entity/Q28070759

description

2016 nî lūn-bûn

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2016 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2016年の論文

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2016年論文

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2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

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name

Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

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Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

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Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

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type

label

Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

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Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

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Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

@nl

prefLabel

Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

@ast

Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

@en

Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

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FMOLB.2016.00054

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Frontiers in molecular biosciences

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Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

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P2093

Darren J. Hart

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Denis Bouvier

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Elise Delaforge

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Jie-rong Huang

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Martin Blackledge

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Sigrid Milles

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P2860

Intrinsically unstructured proteins and their functions

Structural Ensemble of an Intrinsically Disordered Polypeptide

Function and structure of inherently disordered proteins

The Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD / NMR study

Insights into domain-domain motions in proteins and RNA from solution NMR

Crystal structure of the RNA-dependent RNA polymerase from influenza C virus.

Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR

Host Determinant Residue Lysine 627 Lies on the Surface of a Discrete, Folded Domain of Influenza Virus Polymerase PB2 Subunit

Structural Basis of the Influenza A Virus RNA Polymerase PB2 RNA-binding Domain Containing the Pathogenicity-determinant Lysine 627 Residue

Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF

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54

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scholarly article

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3543437

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10.3389/FMOLB.2016.00054

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3

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Malene Ringkjøbing Jensen

Michael Sattler

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2016-09-13T00:00:00Z

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27679800

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5020063

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