Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy
about
High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy.Revealing protein structures in solid-phase peptide synthesis by 13C solid-state NMR: evidence of excessive misfolding for Alzheimer's β.Towards revealing the structure of bacterial inclusion bodies.Molecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy.Effect of chemical chaperones in improving the solubility of recombinant proteins in Escherichia coliA new understanding of antibiotic action via solid-state NMR of cells with uniform isotopic labeling.Analysis of the Aspergillus fumigatus Biofilm Extracellular Matrix by Solid-State Nuclear Magnetic Resonance Spectroscopy.Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.Protein nuclear magnetic resonance under physiological conditionsRetinal dynamics during light activation of rhodopsin revealed by solid-state NMR spectroscopy.Solid-state NMR spectroscopy on complex biomolecules.Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology.Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Morphological differences between β(2) -microglobulin in fibrils and inclusion bodies.Why and how protein aggregation has to be studied in vivo.NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Solid-state nuclear magnetic resonance (NMR) spectroscopy of human immunodeficiency virus gp41 protein that includes the fusion peptide: NMR detection of recombinant Fgp41 in inclusion bodies in whole bacterial cells and structural characterization oIn-Cell Solid-State NMR as a Tool to Study Proteins in Large Complexes
P2860
Q30156069-5F7084E8-51DF-49C8-8F2E-8DD4ECF8FF78Q30373906-AF43A500-F08C-4ACE-9FD6-43DB9A9108A9Q30401276-4D94F67C-D63A-4FF2-A105-C40D64DAC05FQ30412233-33434EC0-34F9-46A9-9481-C912E80E9B3BQ34612503-9E689A9E-98AB-425E-8CEB-798148213BFAQ34779975-03F9669D-DBE9-4A50-BB10-78E95825D386Q35081042-D26A7E29-3017-4F13-9749-01CC90ED95CCQ35221903-CA2A1A4A-B371-4466-AF47-3B397682938FQ36208870-7DD9DFB7-83EA-4A6F-9293-5FE8C090766FQ37074027-20EDFE75-B196-49A9-84AB-3DADAFF80F2EQ37104114-CFF67FD2-6B2E-4F4E-87BA-D6C1ACD5B4AFQ37589121-B2BC8C3A-C596-4DCF-947A-5B9E9B62A74AQ37799776-43F75BF1-4FD0-4A9C-BFC5-DA5E487635C1Q37875224-028D24A5-A909-4FC8-A1F2-11D55E85E0D8Q39017883-3ABE45D6-4DDF-4F3B-9566-F97824D08471Q41878010-C5362597-D921-46EE-BD20-4267FFC76996Q43238672-11759A84-241F-4929-B69C-B91C49C6A57FQ47389447-BBF16914-15A8-454D-BDFD-7E20D4922FBBQ56979426-12104937-DEB3-4AFC-8724-7DF33B23B6D6Q57903640-AA793814-7F5B-463D-B9DD-E0DE42EB5A27
P2860
Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy
description
2008 nî lūn-bûn
@nan
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
2008年论文
@zh
2008年论文
@zh-cn
name
Native conformation at specifi ...... h solid-state NMR spectroscopy
@en
type
label
Native conformation at specifi ...... h solid-state NMR spectroscopy
@en
prefLabel
Native conformation at specifi ...... h solid-state NMR spectroscopy
@en
P2093
P2860
P356
P1476
Native conformation at specifi ...... h solid-state NMR spectroscopy
@en
P2093
David P Weliky
Jaime Curtis-Fisk
Ryan M Spencer
P2860
P304
12568-12569
P356
10.1021/JA8039426
P407
P577
2008-08-29T00:00:00Z