[NMR paper] Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin
Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin
In this paper, we show that the combination of NMR theoretical and experimental results can help to solve the molecular structure of peptides, here it is used as an example the residue Leucine-67 in Desulfovibrio vulgaris flavodoxin. We apply a computational protocol based on the leucine amino acid dipeptide, which, using calculated and experimental spin-spin coupling constants, allows us to obtain the conformation of the...
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[NMR paper] Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin.
Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--academic.oup.com-images-oup_pubmed.png Related Articles Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in Desulfovibrio vulgaris flavodoxin.
Brief Bioinform. 2021 Feb 11;:
Authors: San Fabián J, Omar S, García de la Vega JM
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[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
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...
Probing amino acid side chains of the integral membrane protein PagP by solution NMR: Side chain immobilization ... - ScienceDirect
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