[ASAP] Structural Insights into How Protein Environments Tune the Spectroscopic Properties of a Noncanonical Amino Acid Fluorophore
Structural Insights into How Protein Environments Tune the Spectroscopic Properties of a Noncanonical Amino Acid Fluorophore
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00474/20200903/images/medium/bi0c00474_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00474
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[NMR paper] Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.
Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.
Related Articles Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.
Sci Rep. 2017 Sep 04;7(1):10339
Authors: Mukherjee S, Pondaven SP, Hand K, Madine J, Jaroniec CP
Abstract
The conformational dynamics of a pathogenic ?4 human immunoglobulin light-chain variable domain, SMA, associated with AL...
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09-06-2017 04:13 PM
[NMR paper] The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study.
The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study.
The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study.
Molecules. 2013;18(10):12396-12414
Authors: Medici S, Peana M, Nurchi VM, Zoroddu MA
Abstract
Coordination of proteins and peptides to metal ions is known to affect their properties, often by a change in their structural organization. Side chains of the residues directly involved in metal binding or very close to the coordination centre...
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10-11-2013 10:43 AM
[NMR paper] Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Related Articles Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
J Biol Chem. 2013 Jan 22;
Authors: De Sa Peixoto P, Laurent G, Azais T, Mosser G
Abstract
In vivo, collagen I, the major structural protein in human body, is found assembled into fibrils. In the present work, we study a high concentrated collagen sample in its soluble, fibrillar and denatured states...
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02-03-2013 10:19 AM
4D APSY-HBCB(CG)CDHD experiment for automated assignment of aromatic amino acid side chains in proteins
4D APSY-HBCB(CG)CDHD experiment for automated assignment of aromatic amino acid side chains in proteins
Abstract A four-dimensional (4D) APSY (automated projection spectroscopy)-HBCB(CG)CDHD experiment is presented. This 4D experiment correlates aromatic with aliphatic carbon and proton resonances from the same amino acid side chain of proteins in aqueous solution. It thus allows unambiguous sequence-specific assignment of aromatic amino acid ring signals based on backbone assignments. Compared to conventional 2D approaches, the inclusion of evolution periods on 1Hβ and 13Cδ...
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09-30-2011 08:01 PM
[NMR paper] NMR solution structure of attractin, a water-borne protein pheromone from the mollusk
NMR solution structure of attractin, a water-borne protein pheromone from the mollusk Aplysia californica.
Related Articles NMR solution structure of attractin, a water-borne protein pheromone from the mollusk Aplysia californica.
Biochemistry. 2003 Aug 26;42(33):9970-9
Authors: Garimella R, Xu Y, Schein CH, Rajarathnam K, Nagle GT, Painter SD, Braun W
Water-borne protein pheromones are essential for coordination of reproductive activities in many marine organisms. In this paper, we describe the first structure of a pheromone protein from a...
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11-24-2010 09:16 PM
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D [1H,1H]-NOESY
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D -NOESY
Francesco Fiorito, Torsten Herrmann, Fred F. Damberger and Kurt Wüthrich
Journal of Biomolecular NMR; 2008; 42(1); pp 23-33
Abstract
ASCAN is a new algorithm for automatic sequence-specific NMR assignment of amino acid side-chains in proteins, which uses as input the primary structure of the protein, chemical shift lists of 1HN, 15N, 13Cα, 13Cβ and possibly 1Hα from the previous polypeptide backbone assignment, and one or several 3D 13C- or 15N-resolved -NOESY spectra. ASCAN has also been...
![[ASAP] The Burden Borne by Protein Methyltransferases: Rates and Equilibria of Non-enzymatic Methylation of Amino Acid Side Chains by SAM in Water](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-burden-borne-protein-methyltransferases-rates-equilibria-non-enzymatic-methylation-amino-acid-side-chains-sam-water_ltr.gif)
[ASAP] The Burden Borne by Protein Methyltransferases: Rates and Equilibria of Non-enzymatic Methylation of Amino Acid Side Chains by SAM in Water
Linear Mode
