Experimental approaches for NMR studies of side-chain dynamics in high-molecular-weight proteins

被引：53
|
作者：
Sheppard, Devon [1 ]
Sprangers, Remco [2 ]
Tugarinov, Vitali [1 ]
机构：
[1] Univ Maryland, Dept Chem & Biochem, College Pk, MD 20742 USA
[2] Max Planck Inst Dev Biol, D-72076 Tubingen, Germany
来源：
PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY | 2010年 / 56卷 / 01期
关键词：
Side-chain dynamics; NMR of large proteins; Selective isotope labeling; Methyl-TROSY; Spin relaxation; NUCLEAR-MAGNETIC-RESONANCE; MALATE-SYNTHASE-G; TIME-SCALE DYNAMICS; CHARACTERIZING CHEMICAL-EXCHANGE; HETERONUCLEAR TRANSVERSE RELAXATION; OPTIMIZED SPECTROSCOPY TROSY; CROSS-CORRELATED RELAXATION; DEUTERIUM SPIN PROBES; METHYL-GROUP DYNAMICS; MODEL-FREE APPROACH;
D O I：
10.1016/j.pnmrs.2009.07.004
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
A study was conducted to demonstrate experimental approaches for nuclear magnetic resonance (NMR) studies of side-chain dynamics in high-molecular-weight proteins. The investigations emphasized on spectroscopic NMR approaches and associated isotope labeling strategies that made such large protein assemblies amenable to quantitative NMR studies. The delay elements in NMR pulse-schemes were selected without concern about evolution due to 13C-13C one-bond scalar couplings, leading to improvements in sensitivity. The methyl-selective 13C enrichment was possible through the use of [12C, 2H]-labeled glucose as the main carbon source in minimal media for protein production.
引用
收藏
页码：1 / 45
页数：45
相关论文
共 50 条
  • [21] Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy
    Vitali Tugarinov
    Voula Kanelis
    Lewis E Kay
    Nature Protocols, 2006, 1 : 749 - 754
  • [22] High-molecular-weight side-chain liquid-crystalline polyethers based on 4′-cyanobiphenyl-4-oxy mesogenic groups
    Montornés, JM
    Reina, JA
    Ronda, JC
    JOURNAL OF POLYMER SCIENCE PART A-POLYMER CHEMISTRY, 2004, 42 (12) : 3002 - 3012
  • [23] C-13 NMR-STUDIES OF TRYPTOPHAN SIDE-CHAIN DYNAMICS IN HYDROPHOBIC OLIGOPEPTIDES
    WEAVER, AJ
    KEMPLE, M
    WASSALL, S
    PRENDERGAST, FG
    BIOPHYSICAL JOURNAL, 1987, 51 (02) : A71 - A71
  • [24] Leucine Side-Chain Conformation and Dynamics in Proteins from 13C NMR Chemical Shifts
    Mulder, Frans A. A.
    CHEMBIOCHEM, 2009, 10 (09) : 1477 - 1479
  • [25] A COMPARISON OF 3 THEORETICAL APPROACHES TO THE STUDY OF SIDE-CHAIN INTERACTIONS IN PROTEINS
    MITCHELL, JBO
    NANDI, CL
    THORNTON, JM
    PRICE, SL
    SINGH, J
    SNAREY, M
    JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS, 1993, 89 (15): : 2619 - 2630
  • [26] The utility of small nutation angle 1H pulses for NMR studies of methyl-containing side-chain dynamics in proteins
    Tugarinov, Vitali
    Clore, G. Marius
    PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, 2024, 144 : 40 - 62
  • [27] CHARACTERIZATION OF HIGH-MOLECULAR-WEIGHT AMYLOID-A PROTEINS
    PRELLI, F
    PRAS, M
    SHTRASBURG, S
    FRANGIONE, B
    SCANDINAVIAN JOURNAL OF IMMUNOLOGY, 1991, 33 (06) : 783 - 786
  • [28] HIGH-MOLECULAR-WEIGHT COMPONENT OF THE NEUROFILAMENT PROTEINS IN THE PERIKARYON
    YAMAMOTO, A
    SATAKE, M
    TOYOSHIMA, I
    MIYATAKE, T
    FUJITA, S
    NEUROCHEMICAL RESEARCH, 1986, 11 (12) : 1765 - 1765
  • [29] ELECTROPHORETIC TRANSFER OF HIGH-MOLECULAR-WEIGHT PROTEINS FOR IMMUNOSTAINING
    WANG, K
    FANGER, BO
    GUYER, CA
    STAROS, JV
    METHODS IN ENZYMOLOGY, 1989, 172 : 687 - 696
  • [30] Fitting Side-Chain NMR Relaxation Data Using Molecular Simulations
    Kummerer, Felix
    Orioli, Simone
    Harding-Larsen, David
    Hoffmann, Falk
    Gavrilov, Yulian
    Teilum, Kaare
    Lindorff-Larsen, Kresten
    JOURNAL OF CHEMICAL THEORY AND COMPUTATION, 2021, 17 (08) : 5262 - 5275
12345