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Article

18 Citations

6,255 Views

22 Pages

Reversible Oxidative Modifications in Myoglobin and Functional Implications

Mark H. Mannino,
Rishi S. Patel,
Amanda M. Eccardt,
Blythe E. Janowiak,
David C. Wood,
Fahu He and
Jonathan S. Fisher

Antioxidants2020, 9(6), 549;https://doi.org/10.3390/antiox9060549

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24 June 2020

Myoglobin (Mb), an oxygen-binding heme protein highly expressed in heart and skeletal muscle, has been shown to undergo oxidative modifications on both an inter- and intramolecular level when exposed to hydrogen peroxide (H2O2) in vitro. Here, we sho...

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Feature Paper
Review

67 Citations

11,717 Views

31 Pages

Oxidative Crosslinking of Peptides and Proteins: Mechanisms of Formation, Detection, Characterization and Quantification

Eduardo Fuentes-Lemus,
Per Hägglund,
Camilo López-Alarcón and
Michael J. Davies

Molecules2022, 27(1), 15;https://doi.org/10.3390/molecules27010015

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21 December 2021

Covalent crosslinks within or between proteins play a key role in determining the structure and function of proteins. Some of these are formed intentionally by either enzymatic or molecular reactions and are critical to normal physiological function....

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Article

20 Citations

5,123 Views

9 Pages

In Silico Molecular Study of Tryptophan Bitterness

Antonella Di Pizio and
Alessandro Nicoli

Molecules2020, 25(20), 4623;https://doi.org/10.3390/molecules25204623

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11 October 2020

Tryptophan is an essential amino acid, required for the production of serotonin. It is the most bitter amino acid and its bitterness was found to be mediated by the bitter taste receptor TAS2R4. Di-tryptophan has a different selectivity profile and w...

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