Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR.
Sci Adv. 2016 Aug;2(8):e1600379
Authors: Lange S, Franks WT, Rajagopalan N, Döring K, Geiger MA, Linden A, van Rossum BJ, Kramer G, Bukau B, Oschkinat H
Abstract
Proteins are synthesized in cells by ribosomes and, in parallel, prepared for folding or targeting. While ribosomal protein synthesis is progressing, the nascent chain exposes amino-terminal signal sequences or transmembrane domains that mediate interactions with specific interaction partners, such as the signal recognition particle (SRP), the SecA-adenosine triphosphatase, or the trigger factor. These binding events can set the course for folding in the cytoplasm and translocation across or insertion into membranes. A distinction of the respective pathways depends largely on the hydrophobicity of the recognition sequence. Hydrophobic transmembrane domains stabilize SRP binding, whereas less hydrophobic signal sequences, typical for periplasmic and outer membrane proteins, stimulate SecA binding and disfavor SRP interactions. In this context, the formation of helical structures of signal peptides within the ribosome was considered to be an important factor. We applied dynamic nuclear polarization magic-angle spinning nuclear magnetic resonance to investigate the conformational states of the disulfide oxidoreductase A (DsbA) signal peptide stalled within the exit tunnel of the ribosome. Our results suggest that the nascent chain comprising the DsbA signal sequence adopts an extended structure in the ribosome with only minor populations of helical structure.
Solid-state NMR enhanced by dynamic nuclear polarization as a novel tool for ribosome structural biology
From The DNP-NMR Blog:
Solid-state NMR enhanced by dynamic nuclear polarization as a novel tool for ribosome structural biology
Gelis, I., et al., Solid-state NMR enhanced by dynamic nuclear polarization as a novel tool for ribosome structural biology. J. Biomol. NMR, 2013. 56(2): p. 85-93.
http://dx.doi.org/10.1007/s10858-013-9721-2
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
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Authors: Long F, Cho W, Ishii Y
Amyloid fibrils of Alzheimer's ?-amyloid peptide (A?) are a primary component of amyloid plaques, a hallmark of Alzheimer's disease (AD). Enormous attention has been given to the structural...
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06-07-2011 11:05 AM
[NMR paper] NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.
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gp120 is a subunit of the Env (viral envelope protein) of HIV-1. The protein consists of inner and outer domains linked by a bridging sheet. Several gp120 residues that bind the neutralizing antibody 17b as well as the...
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[NMR paper] Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-label
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J Biomol NMR. 2004 Apr;28(4):311-25
Authors: Fujiwara T, Todokoro Y, Yanagishita H, Tawarayama M, Kohno T, Wakamatsu K, Akutsu H
Carbon-13 and nitrogen-15 signals of fully...
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[NMR paper] Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy an
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Biochemistry. 1994 Jan 11;33(1):33-41
Authors: Jarvis JA, Munro SL, Craik DJ
A peptide corresponding to the amino acid region 71-93 of the plasma protein transthyretin (TTR) has been synthesized to investigate its role in the native...
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08-22-2010 03:33 AM
[NMR paper] Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy an
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Biochemistry. 1994 Jan 11;33(1):33-41
Authors: Jarvis JA, Munro SL, Craik DJ
A peptide corresponding to the amino acid region 71-93 of the plasma protein transthyretin (TTR) has been synthesized to investigate its role in the native...
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08-22-2010 03:33 AM
[NMR paper] 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
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Biochemistry. 1990 Oct 23;29(42):9872-8
Authors: Karslake C, Piotto ME, Pak YK, Weiner H, Gorenstein DG
The 19 amino acid signal peptide of rat liver aldehyde dehydrogenase, possessing a lysine substitution for an arginine and containing 3 extra amino acid residues at the C terminus, was studied by two-dimensional NMR in a dodecylphosphocholine micelle. In this...