about
Nuclear Magnetic Resonance Structure Shows that the Severe Acute Respiratory Syndrome Coronavirus-Unique Domain Contains a Macrodomain FoldSARS Coronavirus Unique Domain: Three-Domain Molecular Architecture in Solution and RNA BindingNMR structure of the protein NP_247299.1: comparison with the crystal structureComparison of NMR and crystal structures for the proteins TM1112 and TM1367The J-UNIO protocol for automated protein structure determination by NMR in solutionNMRFAM-SDF: a protein structure determination frameworkIncreasing the Chemical-Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift ReagentFast acquisition of high resolution 4-D amide-amide NOESY with diagonal suppression, sparse sampling and FFT-CLEAN.NMR-profiles of protein solutionsThe relaxin receptor (RXFP1) utilizes hydrophobic moieties on a signaling surface of its N-terminal low density lipoprotein class A module to mediate receptor activation.APSY-NMR for protein backbone assignment in high-throughput structural biology.Structural proteomics by NMR spectroscopy.Unique opportunities for NMR methods in structural genomics.Advances in Nuclear Magnetic Resonance for Drug Discovery.NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.NMR in a crystallography-based high-throughput protein structure-determination environmentError tolerant NMR backbone resonance assignment and automated structure generation.Advances in automated NMR protein structure determination.4D solid-state NMR for protein structure determination.PACSY, a relational database management system for protein structure and chemical shift analysisA time-saving strategy for MAS NMR spectroscopy by combining nonuniform sampling and paramagnetic relaxation assisted condensed data collection4D experiments measured with APSY for automated backbone resonance assignments of large proteins.ADAPT-NMR 3.0: utilization of BEST-type triple-resonance NMR experiments to accelerate the process of data collection and assignment.Non-uniform sampling: post-Fourier era of NMR data collection and processing.Clean absorption-mode NMR data acquisition.Automated resonance assignment of proteins: 6D APSY-NMR.Biomolecular NMR data analysisA practical implementation of cross-spectrum in protein backbone resonance assignmentCompressed sensing and the reconstruction of ultrafast 2D NMR data: Principles and biomolecular applications.Maximum Entropy Spectral Reconstruction of Non-Uniformly Sampled Data.Data sampling in multidimensional NMR: fundamentals and strategies.Spatially selective heteronuclear multiple-quantum coherence spectroscopy for biomolecular NMR studies.Al NMR: a novel NMR data processing program optimized for sparse sampling.Sensitivity gains, linearity, and spectral reproducibility in nonuniformly sampled multidimensional MAS NMR spectra of high dynamic rangeRadial sampling for fast NMR: Concepts and practices over three decades.AUTOBA: automation of backbone assignment from HN(C)N suite of experiments.Sparsely sampled high-resolution 4-D experiments for efficient backbone resonance assignment of disordered proteinsStructural plasticity in human heterochromatin protein 1βStructural representative of the protein family PF14466 has a new fold and establishes links with the C2 and PLAT domains from the widely distant Pfams PF00168 and PF01477NMR structure determination of the protein NP_344798.1 as the first representative of Pfam PF06042
P2860
Q27653024-5F1D6C7C-5EF1-4E2A-AB1E-E8C172129E10Q27661782-032A9203-B672-4140-9CBB-AAE6BAD0B790Q27665000-57D54931-7717-4CB6-9F7B-690C4BEB74D7Q27665002-4E4A292C-1A85-41A3-BFEF-D6DCB16F8714Q27670598-8972CE49-74BB-4475-98DB-A2FE092ECE60Q28607677-CFF696F7-CBBF-42DB-8CE4-C04E01D23C37Q28817697-695A1B3F-8529-43D3-9683-849AB1269ADAQ30156927-0117EFAC-5BEF-446C-A1E6-4B802A46906BQ30351981-E16C6DF9-A958-4FEC-A8BC-1F34E5CA13EBQ30352669-47200FFA-DE3B-4D61-A516-E2CE86E9EDA8Q30368973-17193FB3-ADF7-4F14-BB64-E3642E05D995Q30371763-A6EAB5DC-8600-4109-9B97-00FBE387B5D5Q30375573-B471E2A9-2717-49C1-9792-7DCB8C241E69Q30387229-E2DC477A-2F19-4E03-8264-ACDFB9CDB17FQ30387827-7D9D3674-660C-498C-BC1E-0E11E58E02C0Q30394839-78A36A35-ACC1-4F6C-B405-5410A5C6C3C7Q30399816-6B4552E7-1D01-4BB1-801B-2508A2B166F9Q30400806-8A1648A0-F52C-46DE-8239-E3E913115712Q30414061-9EC21FAD-C78F-498A-B988-C102C3218CFAQ30420441-4374E36F-A89E-4F23-BBA1-219F97307229Q30574596-D3F1CDEF-9751-48EC-978A-4C9BD0D78115Q30620375-8FA55BA7-570F-41AE-892F-41EE216A47FEQ30960768-F67D7C77-DED3-4E8B-A48D-AC3B1094315BQ30988274-22784FAB-5E36-48F7-BE89-5F98ED68C84EQ33399454-408F3081-4DF4-4813-8E54-E4C00762698FQ33560810-5BCF830F-9F67-4498-876B-94FA2A2863C1Q33631189-0AC32A62-4799-4BF7-9728-19BA6397A4E9Q33746504-7DB28BA8-302E-4270-B7FE-41D51D4ACAD6Q33819086-5260A6E3-0940-4541-99E3-1D77684BA9FCQ33895990-572E973F-4C4B-4971-A35C-73DC8C0FA916Q33966119-D6F4296B-A0A5-48D1-B7BB-4B33C6AB4564Q34003154-C4D594EF-DF38-4CFF-8AFC-A6689F709B3FQ34074527-71F98DAC-C022-46E7-A8B5-84D1C2238C0FQ34079485-BB3B18C4-3EDE-42DA-AF09-4F1112B53179Q34184274-1009E66B-492F-4B55-855B-CAD428F34B06Q34188442-77143FE5-3B37-4947-810D-7F254817B282Q34624640-A6A5E9E9-C251-4FD7-A347-BFF6AA2D482DQ34667860-833DCB39-776A-4B20-AD14-51FDD27B0CB1Q34726947-30712DEA-C159-481D-AB9E-CF4ADC784233Q35007462-18C52F18-D832-4FB2-AA83-98160C441603
P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Automated projection spectroscopy (APSY).
@ast
Automated projection spectroscopy (APSY).
@en
type
label
Automated projection spectroscopy (APSY).
@ast
Automated projection spectroscopy (APSY).
@en
prefLabel
Automated projection spectroscopy (APSY).
@ast
Automated projection spectroscopy (APSY).
@en
P2860
P50
P356
P1476
Automated projection spectroscopy (APSY).
@en
P2093
Francesco Fiorito
P2860
P304
10876-10881
P356
10.1073/PNAS.0504818102
P407
P577
2005-07-25T00:00:00Z