Structural biology by NMR: structure, dynamics, and interactions.
about
Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopyMOTOR: model assisted software for NMR structure determination.Ensemble-based interpretations of NMR structural data to describe protein internal dynamics.CABS-flex predictions of protein flexibility compared with NMR ensembles.Low complexity and disordered regions of proteins have different structural and amino acid preferences.Advances in automated NMR protein structure determination.Nuclear magnetic resonance signal chemical shifts and molecular simulations: a multidisciplinary approach to modeling copper protein structures.Blind testing of routine, fully automated determination of protein structures from NMR dataConformational transition of FGFR kinase activation revealed by site-specific unnatural amino acid reporter and single molecule FRET.Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilisCoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.Toward structure determination using membrane-protein nanocrystals and microcrystals.Studying functional dynamics in bio-molecules using accelerated molecular dynamics.Striking HIV-1 Entry by Targeting HIV-1 gp41. But, Where Should We Target?AIM for Allostery: Using the Ising Model to Understand Information Processing and Transmission in Allosteric Biomolecular Systems.Optimization of purification and refolding of the human chemokine receptor CXCR1 improves the stability of proteoliposomes for structure determinationThe charge-dipole pocket: a defining feature of signaling pathway GTPase on/off switches.Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin.Computational molecular biology approaches to ligand-target interactions.A theoretical view of protein dynamics.Protein dynamics: from rattling in a cage to structural relaxation.Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Improved reliability, accuracy and quality in automated NMR structure calculation with ARIA.The description of protein internal motions aids selection of ligand binding poses by the INPHARMA methodDivide and conquer is always best: sensitivity of methyl correlation experiments.From protein sequence to dynamics and disorder with DynaMine.Structural characterization of supramolecular assemblies by ¹³C spin dilution and 3D solid-state NMR.Probing Structural Changes among Analogous Inhibitor-Bound Forms of HIV-1 Protease and a Drug-Resistant Mutant in Solution by Nuclear Magnetic Resonance.Essential dynamics analysis captures the concerted motion of the integrin-binding site in jerdostatin, an RTS disintegrin.Coordination to lanthanide ions distorts binding site conformation in calmodulin.Automated Protein Structure Determination Methods
P2860
Q28474887-99554E32-2227-42FD-8F03-099AD169DB42Q30352079-B63288B5-A364-4632-A3FC-C93DF5890CDAQ30353311-82C16033-A7D1-4690-A5B9-BFF65814F113Q30361384-70E86413-A031-4760-A1D3-6532824920C9Q30369339-100B304D-F5B2-446C-B9F9-A7CC371A0E53Q30400806-DA0D5838-D17B-444D-90A5-AE23ACB6CDBDQ30405971-F16B1749-E458-4E69-B260-1190F301EBCCQ30412925-0561585E-F243-4028-A6AF-EF9A4AA6CE08Q30833549-40E22EC2-CBAD-46D1-A428-BD4EEE880CBFQ33684835-21229C73-91B6-41BD-9018-45E87BBB8CECQ33733627-31BF9A0F-52F5-4D37-B2DC-D35D323363BCQ33819825-62C2E733-6521-4A44-BC65-02BCD64BDCEDQ34111760-4E4F3056-52C0-4628-8BE6-2B4AF35AB90AQ34225993-B922C690-FD0C-4DA4-B598-6E441576FE36Q35898024-C69D5000-4E48-4CBB-B634-7D4CC1491520Q36299381-92C1594C-3C11-441B-B4C8-7CAC4098E020Q37184416-06CA8924-E407-4FD5-82C8-B275F81A7173Q37235510-9E1AA7E5-789F-4573-9995-0895EF366744Q37428879-3E242852-AB97-423C-848C-C42582813364Q37684817-BD4B457D-7D76-4591-AD1A-BAB74037631AQ38202826-E5D4A31D-AAFB-487F-AD20-165446885070Q38509224-2775BF15-2DB9-434E-A574-26B3E7709120Q38578280-DFCED487-2FDF-4A79-A65C-B6AE4589F7A5Q41091068-B16FCEA2-52D2-4E07-BBD9-4B3F618213C9Q41666516-4172948B-C235-4A2F-8015-36B9B80A1A09Q42578396-B36049E3-0E6F-43CB-BD10-5E739EE989ADQ44486815-F885D55F-1945-4568-A663-4B8B37ABEF72Q46764950-3547283E-0F07-4DB6-9973-4FE8B3D9BAF0Q49851708-AF3DC7C7-7415-47A3-ADE7-5767D5F11879Q51686837-2ABF9B94-BAF5-4D1B-B809-3D5DBF2E10ECQ52353920-44441E20-5108-402E-90AE-BB780922B01EQ57902541-09494E21-C4C4-4C77-AC01-5289100C7742
P2860
Structural biology by NMR: structure, dynamics, and interactions.
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structural biology by NMR: structure, dynamics, and interactions.
@ast
Structural biology by NMR: structure, dynamics, and interactions.
@en
type
label
Structural biology by NMR: structure, dynamics, and interactions.
@ast
Structural biology by NMR: structure, dynamics, and interactions.
@en
prefLabel
Structural biology by NMR: structure, dynamics, and interactions.
@ast
Structural biology by NMR: structure, dynamics, and interactions.
@en
P2860
P1476
Structural biology by NMR: structure, dynamics, and interactions.
@en
P2093
Phineus R L Markwick
Thérèse Malliavin
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000168
P577
2008-09-26T00:00:00Z