[NMR paper] Cysteines and Disulfide Bonds as Structure-Forming Units: Insights From Different Domains of Life and the Potential for Characterization by NMR.
Related ArticlesCysteines and Disulfide Bonds as Structure-Forming Units: Insights From Different Domains of Life and the Potential for Characterization by NMR.
Front Chem. 2020;8:280
Authors: Wiedemann C, Kumar A, Lang A, Ohlenschläger O
Abstract
Disulfide bridges establish a fundamental element in the molecular architecture of proteins and peptides which are involved e.g., in basic biological processes or acting as toxins. NMR spectroscopy is one method to characterize the structure of bioactive compounds including cystine-containing molecules. Although the disulfide bridge itself is invisible in NMR, constraints obtained via the neighboring NMR-active nuclei allow to define the underlying conformation and thereby to resolve their functional background. In this mini-review we present shortly the impact of cysteine and disulfide bonds in the proteasome from different domains of life and give a condensed overview of recent NMR applications for the characterization of disulfide-bond containing biomolecules including advantages and limitations of the different approaches.
[NMR paper] MAS NMR detection of hydrogen bonds for protein secondary structure characterization.
MAS NMR detection of hydrogen bonds for protein secondary structure characterization.
Related Articles MAS NMR detection of hydrogen bonds for protein secondary structure characterization.
J Biomol NMR. 2020 Mar 17;:
Authors: Friedrich D, Perodeau J, Nieuwkoop AJ, Oschkinat H
Abstract
Hydrogen bonds are essential for protein structure and function, making experimental access to long-range interactions between amide protons and heteroatoms invaluable. Here we show that measuring distance restraints involving backbone hydrogen...
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MAS NMR detection of hydrogen bonds for protein secondary structure characterization
MAS NMR detection of hydrogen bonds for protein secondary structure characterization
Abstract
Hydrogen bonds are essential for protein structure and function, making experimental access to long-range interactions between amide protons and heteroatoms invaluable. Here we show that measuring distance restraints involving backbone hydrogen atoms and carbonyl- or α-carbons enables the identification of secondary structure elements based on hydrogen bonds, provides long-range contacts and validates spectral assignments. To this end, we apply specifically...
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03-18-2020 10:42 AM
Selenoglutathione Diselenide: Unique Redox Reactionsin the GPx-Like Catalytic Cycle and Repairing of Disulfide Bonds inScrambled Protein
Selenoglutathione Diselenide: Unique Redox Reactionsin the GPx-Like Catalytic Cycle and Repairing of Disulfide Bonds inScrambled Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00751/20171012/images/medium/bi-2017-00751x_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00751
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10-13-2017 06:49 AM
[NMR paper] Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins.
Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins.
Related Articles Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins.
Angew Chem Int Ed Engl. 2017 Sep 17;:
Authors: Ludwig R, Khudozhitkov AE, Stange P, Golub B, Paschek D, Stepanov AG, Kolokolov DI
Abstract
We present the first...
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[NMR paper] Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins
Characterization of doubly ionic hydrogen bonds in protic ionic liquids by NMR deuteron quadrupole coupling constants - Differences to H-bonds in amides, peptides and proteins
We present the first deuteron quadrupole coupling constants (DQCC) for selected protic ionic liquids (PILs) measured by solid-state NMR spectroscopy. The experimental data are supported by dispersion-corrected density functional theory (DFT-D3) calculations and molecular dynamics (MD) simulations. The DQCCs of the N-D bond in the triethylammonium cations are the lowest reported for deuterons in PILs indicating...
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09-18-2017 10:41 AM
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Abstract NOEs between the β-protons of cysteine residues across disulfide bonds in proteins provide direct information on the connectivities and conformations of these important cross-links, which are otherwise difficult to investigate. With conventional -proteins, however, fast spin diffusion processes mediated by strong dipolar interactions between geminal β-protons prohibit the quantitative measurements and thus the analyses of long-range NOEs across...
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[NMR paper] Disulfide bonds in homo- and heterodimers of EF-hand subdomains of calbindin D9k: sta
Disulfide bonds in homo- and heterodimers of EF-hand subdomains of calbindin D9k: stability, calcium binding, and NMR studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Disulfide bonds in homo- and heterodimers of EF-hand subdomains of calbindin D9k: stability, calcium binding, and NMR studies.
Protein Sci. 1993 Jun;2(6):985-1000
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[NMR paper] Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin
Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.
Related Articles Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.
J Biomol NMR. 1991 May;1(1):49-64
Authors: Uchida K, Miyake Y, Kainosho M
Four enhanced carbonyl carbon resonances were observed when Streptomyces subtilisin inhibitor (SSI) was labeled by...
Cysteines and Disulfide Bonds as Structure-Forming Units: Insights From Different Domains of Life and the Potential for Characterization by NMR.
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