H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins.
about
Backbone assignment and secondary structure of the PsbQ protein from photosystem IIMolecular basis of the mixed lineage leukemia-menin interaction: implications for targeting mixed lineage leukemias.Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.Novel strategies for drug discovery based on Intrinsically Disordered Proteins (IDPs)Recent progress in NMR spectroscopy: toward the study of intrinsically disordered proteins of increasing size and complexity.Conformational propensities of intrinsically disordered proteins from NMR chemical shifts.Structural characterization of intrinsically disordered proteins by NMR spectroscopy.Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.CACA-TOCSY with alternate 13C-12C labeling: a 13Calpha direct detection experiment for mainchain resonance assignment, dihedral angle information, and amino acid type identification.High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteinsThe heterogeneous structural behavior of E7 from HPV16 revealed by NMR spectroscopy.TSAR: a program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution spectra.4D non-uniformly sampled HCBCACON and ¹J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins.Direct correlation of consecutive C'-N groups in proteins: a method for the assignment of intrinsically disordered proteins.Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins.NMR spectroscopic studies of intrinsically disordered proteins at near-physiological conditions.Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c.Direct ¹³C-detected NMR experiments for mapping and characterization of hydrogen bonds in RNA.In-cell ¹³C NMR spectroscopy for the study of intrinsically disordered proteins.NMR structure analysis of uniformly 13C-labeled carbohydrates.13C direct-detection biomolecular NMR spectroscopy in living cells.High-dimensionality 13C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR SpectroscopyExclusively Heteronuclear13C-Detected Amino-Acid-Selective NMR Experiments for the Study of Intrinsically Disordered Proteins (IDPs)Intrinsically Disordered ProteinsSpeeding up sequence specific assignment of IDPsHigh-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of 13C-Detected NMR Spectroscopy Experiments to Determine Key Observables
P2860
Q29950661-04C9E6B9-F38D-4CE2-97C3-53C9C3383EB1Q30429228-5A400D0C-F9E4-43AB-AFFC-E924B7A0DB49Q31094030-1EC3B2AD-97DE-479C-92EB-1DE474044184Q37891686-09CB5204-2FC6-4864-86B4-93FF6F438833Q38007407-CCF89384-9255-40EB-A7EE-46A14E46EFCEQ38116495-C7D37B49-402A-4FB4-A545-008DC9DBD513Q38134535-DC46EEB8-F733-4BD8-AA17-F3A7B8213AF8Q40216589-3D3E978B-4432-4B7C-8431-942691FFDB70Q40498144-996E3129-741D-4E50-B7AE-784678F92E02Q41971008-7068D66D-9C0A-4769-8345-A8ED4A94635EQ42277084-18D8459B-C1AA-4842-BED4-8E7245E5F4DEQ43406107-3BF2E3E2-F71B-405C-ABE4-53A1D217840AQ44137029-8F73972C-4FB3-4DF7-BC26-0CFB01E2D2C0Q44310516-5912775A-BBA8-489B-AFF8-A54A57F61CCCQ44567650-A9C27D43-CAAB-4D84-9224-05832BC4AB81Q46854196-26D4965D-06AC-4CBF-B811-D58E535B4E6AQ47955285-26624F6D-1B49-4B98-BCC6-607E090E7272Q48245320-20D2046B-968F-4368-A8BF-D54858CBED42Q48285708-467594CF-42E6-4E9C-BCDE-BEB0446F3B21Q54290264-03F64B03-9325-4FE9-B062-612BEE64D167Q54367556-88B46734-9251-4078-9442-9019A76DF777Q54644975-B74AF1D7-F836-41E0-A02D-019F92DA32A3Q57837623-E70465FD-DADE-4A27-9908-D3C098F77BD3Q57976405-4AD64817-46BF-4F65-BEE9-F4DEDD0EAAC8Q57976407-BDE1BA8E-470A-4A68-8FA7-922140C4D5F6Q57976414-6296B080-F25D-4D3C-A48E-412D55C1947BQ57976419-8C6D88E4-299C-443D-9872-53450C93DC94
P2860
H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
H-start for exclusively hetero ...... insically disordered proteins.
@en
H-start for exclusively hetero ...... insically disordered proteins.
@nl
type
label
H-start for exclusively hetero ...... insically disordered proteins.
@en
H-start for exclusively hetero ...... insically disordered proteins.
@nl
prefLabel
H-start for exclusively hetero ...... insically disordered proteins.
@en
H-start for exclusively hetero ...... insically disordered proteins.
@nl
P2093
P50
P1476
H-start for exclusively hetero ...... insically disordered proteins.
@en
P2093
Peter Tompa
Veronika Csizmok
Wolfgang Bermel
P304
P356
10.1016/J.JMR.2009.02.012
P577
2009-03-04T00:00:00Z