In-Cell NMR Spectroscopy of Intrinsically Disordered Proteins

被引：17
作者：
Sciolino, Nicholas [1 ]
Burz, David S. [1 ]
Shekhtman, Alexander [1 ]
机构：
[1] SUNY Albany, Dept Chem, Albany, NY 12222 USA
来源：
PROTEOMICS | 2019年 / 19卷 / 06期
关键词：
in-cell NMR; Mycobacterium tuberculosis; NMR spectroscopy; protein-protein interactions; synuclein; UBIQUITIN-LIKE PROTEIN; HUMAN ALPHA-SYNUCLEIN; A-BETA COMPONENT; MYCOBACTERIUM-TUBERCULOSIS; ESCHERICHIA-COLI; ALZHEIMERS-DISEASE; QUINARY INTERACTIONS; SECONDARY STRUCTURE; BACKBONE DYNAMICS; HYDROGEN-EXCHANGE;
D O I：
10.1002/pmic.201800055
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
This review summarizes the results of in-cell Nuclear Magnetic Resonance, NMR, spectroscopic investigations of the eukaryotic and prokaryotic intrinsically disordered proteins, IDPs: alpha-synuclein, prokaryotic ubiquitin-like protein, Pup, tubulin-related neuronal protein, Tau, phenylalanyl-glycyl-repeat-rich nucleoporins, FG Nups, and the negative regulator of flagellin synthesis, FlgM. The results show that the cellular behavior of IDPs may differ significantly from that observed in the test tube.
引用
收藏
页数：16
相关论文
共 152 条
[1]  
Alderson T Reid, 2013, Intrinsically Disord Proteins, V1, P18, DOI 10.4161/idp.26255
[2]   Determination of the Free Energy Landscape of α-Synuclein Using Spin Label Nuclear Magnetic Resonance Measurements [J].
Allison, Jane R. ;
Varnai, Peter ;
Dobson, Christopher M. ;
Vendruscolo, Michele .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2009, 131 (51) :18314-18326
[3]   Phosphorylation of Ser-129 is the dominant pathological modification of α-synuclein in familial and sporadic Lewy body disease [J].
Anderson, John P. ;
Walker, Donald E. ;
Goldstein, Jason M. ;
de laat, Rian ;
Banducci, Kelly ;
Caccavello, Russell J. ;
Barbour, Robin ;
Huang, Jiping ;
Kling, Kristin ;
Lee, Michael ;
Diep, Linnea ;
Keim, Pamela S. ;
Shen, Xiaofeng ;
Chataway, Tim ;
Schlossmacher, Michael G. ;
Seubert, Peter ;
Schenk, Dale ;
Sinha, Sukanto ;
Gai, Wei Ping ;
Chilcote, Tamie J. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (40) :29739-29752
[4]  
[Anonymous], 2012, MATRIX COMPUTATIONS
[5]   PRIMARY STRUCTURE EFFECTS ON PEPTIDE GROUP HYDROGEN-EXCHANGE [J].
BAI, YW ;
MILNE, JS ;
MAYNE, L ;
ENGLANDER, SW .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1993, 17 (01) :75-86
[6]  
Banci L, 2013, NAT CHEM BIOL, V9, P297, DOI [10.1038/NCHEMBIO.1202, 10.1038/nchembio.1202]
[7]   BACKBONE DYNAMICS OF CALMODULIN STUDIED BY N-15 RELAXATION USING INVERSE DETECTED 2-DIMENSIONAL NMR-SPECTROSCOPY - THE CENTRAL HELIX IS FLEXIBLE [J].
BARBATO, G ;
IKURA, M ;
KAY, LE ;
PASTOR, RW ;
BAX, A .
BIOCHEMISTRY, 1992, 31 (23) :5269-5278
[8]   Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells [J].
Barbieri, Letizia ;
Luchinat, Enrico ;
Banci, Lucia .
NATURE PROTOCOLS, 2016, 11 (06) :1101-1111
[9]   Internal and Global Protein Motion Assessed with a Fusion Construct and In-Cell NMR Spectroscopy [J].
Barnes, Christopher O. ;
Monteith, William B. ;
Pielak, Gary J. .
CHEMBIOCHEM, 2011, 12 (03) :390-391
[10]   In-cell protein NMR and protein leakage [J].
Barnes, Christopher O. ;
Pielak, Gary J. .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2011, 79 (02) :347-351
12345678910