About: The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration 1 1 Edited by P.E.Wright

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About: The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration 1 1 Edited by P.E.Wright Goto Sponge NotDistinct Permalink

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description	article (en) wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 1997 (uk) article scientifique publié en 1997 (fr) im Februar 1997 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q58175598-2AAF364A-27DD-4C6C-A6EA-A010CC6CB344
publication date	1997-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58175598-7318DD86-6551-4F4A-807F-2C11CDF83C46
language of work or name	English
author name string	wds:Q58175598-D2AAA3A2-65BB-4A68-8D45-EAB86E5AAAA5 wds:Q58175598-E5633C2C-64DC-4640-88E0-E6BAFF289D3E
author name string	David Fushman Sean Cahill
rdfs:label	The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration 1 1 Edited by P.E.Wright (en) The main-chain dynamics of the dynamin pleckstrin homology (nl)
skos:prefLabel	The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration 1 1 Edited by P.E.Wright (en) The main-chain dynamics of the dynamin pleckstrin homology (nl)
name	The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration 1 1 Edited by P.E.Wright (en) The main-chain dynamics of the dynamin pleckstrin homology (nl)
author	wds:Q58175598-915B2A96-5765-4746-91BA-BF2611631F53
author	David Cowburn
title	wds:Q58175598-F5B2B833-8CF7-40B8-A666-5DE580C82E1C
title	The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration 1 1 Edited by P.E.Wright (en)
page(s)	wds:Q58175598-92286CAB-3B07-4FB6-9866-DD336A3C7132
page(s)	173-194
instance of	wds:Q58175598-11A03AE4-4F68-4B45-980C-5577D4FDBB72
instance of	scholarly article
PubMed ID	wds:Q58175598-3AECE584-A23D-4294-8EE4-4FD881B66DC1
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9054979
PubMed ID	9054979
published in	wds:Q58175598-A5ED1AB3-7EEF-4B15-9793-A9D94FB500B4
published in	Journal of Molecular Biology
issue	wds:Q58175598-D4FEFCCF-F46F-4511-952B-88350B0112E7
volume	wds:Q58175598-F3A0DFBF-DED9-4BEC-9574-C3C6B2BBFF13
issue	1
volume	266
DOI	wds:Q58175598-701104CD-7064-4636-AF9B-5E8DC9CC159B
DOI	http://dx.doi.org/10.1006/JMBI.1996.0771
DOI	10.1006/JMBI.1996.0771
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58175598
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NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition Mapping the interactions between Lys48 and Lys63-linked di-ubiquitins and a ubiquitin-interacting motif of S5a Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR and MD simulations Novel inhibitors of AKT: assessment of a different approach targeting the pleckstrin homology domain Affinity Makes the Difference: Nonselective Interaction of the UBA Domain of Ubiquilin-1 with Monomeric Ubiquitin and Polyubiquitin Chains Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP1 studied by NMR relaxation. Solution Structure and Backbone Dynamics of Human Liver Fatty Acid Binding Protein: Fatty Acid Binding Revisited Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces Practical aspects of the 2D 15N-[1h]-NOE experiment. Structural properties of polyubiquitin chains in solution Backbone dynamics of SDF-1alpha determined by NMR: interpretation in the presence of monomer-dimer equilibrium Four-alpha-helix bundle with designed anesthetic binding pockets. Part I: structural and dynamical analyses Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein Structural dynamics of bio-macromolecules by NMR: the slowly relaxing local structure approach Variability of the 15N chemical shielding tensors in the B3 domain of protein G from 15N relaxation measurements at several fields. Implications for backbone order parameters Deriving quantitative dynamics information for proteins and RNAs using ROTDIF with a graphical user interface. Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G. Anisotropic rotational diffusion in model-free analysis for a ternary DHFR complex Direct measurement of the 15N CSA/dipolar relaxation interference from coupled HSQC spectra. Backbone dynamics of free barnase and its complex with barstar determined by 15N NMR relaxation study Nuclear magnetic resonance relaxation in determination of residue-specific 15N chemical shift tensors in proteins in solution: protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy. Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins Probing molecular motion by NMR. 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A binding partner of Gbetagamma subunits Protein dynamics from NMR: the slowly relaxing local structure analysis compared with model-free analysis An evaluation of detergents for NMR structural studies of membrane proteins. A comparative study of the backbone dynamics of two closely related lipid binding proteins: bovine heart fatty acid binding protein and porcine ileal lipid binding protein. Hsc70-interacting HPD loop of the J domain of polyomavirus T antigens fluctuates in ps to ns and micros to ms. Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR. NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1 Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists NMR studies of a channel protein without membranes: Structure and dynamics of water-solubilized KcsA NMR structure and dynamics of a designed water-soluble transmembrane domain of nicotinic acetylcholine receptor Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis Model-free model elimination: a new step in the model-free dynamic analysis of NMR relaxation data On the measurement of 15N-{1H} nuclear Overhauser effects The Pleckstrin Homology Domains of Dynamin Isoforms Require Oligomerization for High Affinity Phosphoinositide Binding Characterization of binding-induced changes in dynamics suggests a model for sequence-nonspecific binding of ssDNA by replication protein A. Azido and diazarinyl analogues of bis-tyrphostin as asymmetrical inhibitors of dynamin GTPase The molecular mechanism of nuclear transport revealed by atomic-scale measurements Capping motifs stabilize the leucine-rich repeat protein PP32 and rigidify adjacent repeats Using NMR spectroscopy to monitor ubiquitin chain conformation and interactions with ubiquitin-binding domains. Alanine scan of core positions in ubiquitin reveals links between dynamics, stability, and function On the measurement of ¹⁵N-{¹H} nuclear Overhauser effects. 2. Effects of the saturation scheme and water signal suppression Solution structure and main chain dynamics of the regulatory domain (Residues 1-91) of human cardiac troponin C. Structure and Dynamics of the P7 Protein from the Bacteriophage ϕ12

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