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  • 1
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 30 May 2017, Vol.114(22), pp.E4399-E4407
    Description: Protein biosynthesis is inherently coupled to cotranslational protein folding. Folding of the nascent chain already occurs during synthesis and is mediated by spatial constraints imposed by the ribosomal exit tunnel as well as self-interactions. The polypeptide's vectorial emergence from the ribosomal tunnel establishes the possible folding pathways leading to its native tertiary structure. How cotranslational protein folding and the rate of synthesis are linked to a protein's amino acid sequence is still not well defined. Here, we follow synthesis by individual ribosomes using dual-trap optical tweezers and observe simultaneous folding of the nascent polypeptide chain in real time. We show that observed stalling during translation correlates with slowed peptide bond formation at successive proline sequence positions and electrostatic interactions between positively charged amino acids and the ribosomal tunnel. We also determine possible cotranslational folding sites initiated by hydrophobic collapse for an unstructured and two globular proteins while directly measuring initial cotranslational folding forces. Our study elucidates the intricate relationship among a protein's amino acid sequence, its cotranslational nascent-chain elongation rate, and folding.
    Keywords: Cotranslational Protein Folding ; Optical Tweezers ; Protein Synthesis ; Ribosomes ; Single Molecule ; Protein Biosynthesis ; Protein Folding
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 2
    In: Nature, 2013, Vol.497(7447), p.45
    Keywords: Arrestins -- Chemistry ; Phosphopeptides -- Chemistry ; Protein Isoforms -- Chemistry ; Receptors, Vasopressin -- Chemistry;
    ISSN: 0028-0836
    E-ISSN: 14764687
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  • 3
    Language: English
    In: Nature, 5/2013, Vol.497(7447), pp.45-46
    Description: Many of these interactions are mediated through G-protein-coupled receptors (GPCRs), which in turn activate the eponymous intracellular G proteins, and so act as the starting points for numerous cellular signalling pathways. In the second arrestin paper, Shukla et al.2 (page 137) describe the crystal structure of non-visual β-arrestin-1 in complex with an antibody fragment (Fab30) and a phosphorylated peptide (V2Rpp) that corresponds to 29 amino-acid residues of the C-terminal end of a GPCR (the V2 vasopressin receptor).
    Keywords: Animals–Chemistry ; Arrestins–Metabolism ; Arrestins–Chemistry ; Humans–Metabolism ; Phosphopeptides–Chemistry ; Phosphopeptides–Metabolism ; Protein Isoforms–Chemistry ; Protein Isoforms–Chemistry ; Receptors, Vasopressin–Chemistry ; Proteins ; Studies ; Enzymes ; Crystal Structure ; Cognition & Reasoning ; Crystallization ; Arrestins ; Phosphopeptides ; Protein Isoforms ; Receptors, Vasopressin ; Beta-Arrestin;
    ISSN: 0028-0836
    E-ISSN: 1476-4687
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  • 4
    Language: English
    In: Journal of the American Chemical Society, 18 January 2017, Vol.139(2), pp.985-992
    Description: A meta-terphenyl unit was substituted with an isocyanide group on each of its two terminal aryls to afford a bidentate chelating ligand (CNArNC) that is able to stabilize chromium in its zerovalent oxidation state. The homoleptic Cr(CNArNC) complex luminesces in solution at room temperature, and its excited-state lifetime (2.2 ns in deaerated THF at 20 °C) is nearly 2 orders of magnitude longer than the current record lifetime for isoelectronic Fe(II) complexes, which are of significant interest as earth-abundant sensitizers in dye-sensitized solar cells. Due to its chelating ligands, Cr(CNArNC) is more robust than Cr(0) complexes with carbonyl or monodentate isocyanides, manifesting in comparatively slow photodegradation. In the presence of excess anthracene in solution, efficient energy transfer and subsequent triplet-triplet annihilation upconversion is observed. With an excited-state oxidation potential of -2.43 V vs Fc/Fc, the Cr(0) complex is a very strong photoreductant. The findings presented herein are relevant for replacement of precious metals in dye-sensitized solar cells and in luminescent devices by earth-abundant elements.
    Keywords: Chemistry;
    ISSN: 00027863
    E-ISSN: 1520-5126
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  • 5
    Language: English
    In: Biophysical Journal, 2011, Vol.100(3), pp.404a-404a
    Keywords: Biology
    ISSN: 0006-3495
    E-ISSN: 1542-0086
    Source: ScienceDirect Journals (Elsevier)
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  • 6
    Language: English
    In: Biophysical Journal, 31 January 2012, Vol.102(3), pp.268a-268a
    Keywords: Biology
    ISSN: 0006-3495
    E-ISSN: 1542-0086
    Source: ScienceDirect Journals (Elsevier)
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  • 7
    Language: English
    In: Chemistry (Weinheim an der Bergstrasse, Germany), 27 June 2017, Vol.23(36), pp.8577-8580
    Description: The first two homoleptic Ni isocyanide complexes that exhibit photoluminescence from long-lived excited states are presented. Electrochemical studies indicate that in one of the complexes significant geometrical distortion occurs upon metal oxidation. The observation of luminescence, even though currently restricted to low temperatures, is an important proof-of-concept in the search for earth-abundant alternatives to photoactive complexes made from precious metals. The prospect of using Ni isocyanide complexes as luminophores, photoredox catalysts, or dyes in solar cells, is highly attractive.
    Keywords: Uv/Vis Spectroscopy ; Copper ; Isocyanide Ligands ; Luminescence ; Nickel
    E-ISSN: 1521-3765
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  • 8
    Language: English
    In: Chemistry - A European Journal, 06/27/2017, Vol.23(36), pp.8541-8541
    Description: Byline: Laura A. Buldt, Christopher B. Larsen,Oliver S. Wenger Keywords: copper; isocyanide ligands; luminescence; nickel; UV/Vis spectroscopy Abstract The first two homoleptic Ni.sub.0 isocyanide complexes that exhibit photoluminescence from long-lived excited states are presented. Electrochemical studies indicate that in one of the complexes significant geometrical distortion occurs upon metal oxidation. The observation of luminescence, even though currently restricted to low temperatures, is an important proof-of-concept in the search for earth-abundant alternatives to photoactive complexes made from precious metals. The prospect of using Ni.sub.0 isocyanide complexes as luminophores, photoredox catalysts, or dyes in solar cells, is highly attractive. Supporting information: Additional Supporting Information may be found in the online version of this article As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. CAPTION(S): Supplementary
    Keywords: Chelates;
    ISSN: Chemistry - A European Journal
    E-ISSN: 09476539
    E-ISSN: 15213765
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  • 9
    Language: English
    In: Chemistry - A European Journal, 06/27/2017, Vol.23(36), pp.8539-8539
    Description: Photoluminescence at low temperature was observed for the first time from homoleptic Ni0 isocyanide complexes. The observation of luminescence, even though currently restricted to low temperatures, is an important proof‐of‐concept in the search for earth‐abundant alternatives to photoactive complexes made from precious metals. More information can be found in the Communication by O. S. Wenger et al. on page 8577.
    Keywords: Chemistry;
    ISSN: Chemistry - A European Journal
    E-ISSN: 09476539
    E-ISSN: 15213765
    Source: Wiley (via CrossRef)
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  • 10
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 15 November 2011, Vol.108(46), pp.18690-5
    Description: Arrestins are regulatory molecules for G-protein coupled receptor function. In visual rhodopsin, selective binding of arrestin to the cytoplasmic side of light-activated, phosphorylated rhodopsin (P-Rh*) terminates signaling via the G-protein transducin. While the "phosphate-sensor" of arrestin for the recognition of receptor-attached phosphates is identified, the molecular mechanism of arrestin binding and the involvement of receptor conformations in this process are still largely hypothetic. Here we used fluorescence pump-probe and time-resolved fluorescence depolarization measurements to investigate the kinetics of arrestin conformational changes and the corresponding nanosecond dynamical changes at the receptor surface. We show that at least two sequential conformational changes of arrestin occur upon interaction with P-Rh*, thus providing a kinetic proof for the suggested multistep nature of arrestin binding. At the cytoplasmic surface of P-Rh*, the structural dynamics of the amphipathic helix 8 (H8), connecting transmembrane helix 7 and the phosphorylated C-terminal tail, depends on the arrestin interaction state. We find that a high mobility of H8 is required in the low-affinity (prebinding) but not in the high-affinity binding state. High-affinity arrestin binding is inhibited when a bulky, inflexible group is bound to H8, indicating close interaction. We further show that this close steric interaction of H8 with arrestin is mandatory for the transition from prebinding to high-affinity binding; i.e., for arrestin activation. This finding implies a regulatory role for H8 in activation of visual arrestin, which shows high selectivity to P-Rh* in contrast to the broad receptor specificity displayed by the two nonvisual arrestins.
    Keywords: Arrestin -- Chemistry ; Receptors, G-Protein-Coupled -- Chemistry ; Rhodopsin -- Chemistry
    ISSN: 00278424
    E-ISSN: 1091-6490
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