Nam H. Đào
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Nam H. Đào has a total of 26 co-authors. Here are the top co-authors by number of shared publications:
- Amanda Lestari Gunawan
Department of Nutritional Sciences and Toxicology, University of California, Berkeley, CA, 94720, USA
1 shared publication Amr A. Alazali
Department of Electrical Engineering and Computer Sciences, University of California, Berkeley, Berkeley CA 94720, USA
1 shared publication- Andreas Stahl
Department of Nutrition and Toxicology, University of California Berkeley, Berkeley, USA
1 shared publication - Angel Gonzalez-Valero
Department of Chemistry, University of California, Berkeley, Berkeley, USA
1 shared publication - Annika C. S. Page
Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA
1 shared publication - Audrey G. Reeves
Department of Chemistry, University of California, Berkeley, California 94720, United States
1 shared publication
Latest Publications
- Open Access
- 11 November 2026
- Published by Royal Society of Chemistry (RSC) in Digital Discovery
- Vol. 5 (11) , 4989-5000
Systematic trends in water properties across Jacob's ladder density functionals
Kohn–Sham density functional theory is the workhorse of computational materials science and chemistry, but the optimal choice of exchange–correlation approximation for a given system is often unclear.
- 11 November 2026
- Published by Royal Society of Chemistry (RSC) in Digital Discovery
- Vol. 5 (11) , 4989-5000
Open AccessSystematic trends in water properties across Jacob's ladder density functionals
Kohn–Sham density functional theory is the workhorse of computational materials science and chemistry, but the optimal choice of exchange–correlation approximation for a given system is often unclear.
- Open Access
Chiral methionine oxidation reagents reveal stereospecific proteome modifications
Life is predicated on chirality, a molecular asymmetry akin to the left and right versions of human hands. Here we show that privileged protein residues are predisposed for chiral regulation. We developed enantiomeric oxaziridine reagents that systematically identify pro-( S ) and pro-( R ) methionine oxidation sites across proteomes that can be erased by stereospecific methionine sulfoxide reductase enzymes A and B, respectively. These probes reveal that chiral regulation of methionine oxidation-reduction processes can allosterically regulate protein function, as shown in cell and murine models of oxidative stress where selective ( R )-methionine sulfoxide formation on M69 of biphenyl hydrolase-like protein leads to hydrolase inhibition and amplification of proteome N -homocysteinylation modifications. This work introduces a platform for characterizing sites of asymmetric methionine oxidation and the functional consequences concomitant with an individual chiral single-atom modification.
Open AccessChiral methionine oxidation reagents reveal stereospecific proteome modifications
Life is predicated on chirality, a molecular asymmetry akin to the left and right versions of human hands. Here we show that privileged protein residues are predisposed for chiral regulation. We developed enantiomeric oxaziridine reagents that systematically identify pro-( S ) and pro-( R ) methionine oxidation sites across proteomes that can be erased by stereospecific methionine sulfoxide reductase enzymes A and B, respectively. These probes reveal that chiral regulation of methionine oxidation-reduction processes can allosterically regulate protein function, as shown in cell and murine models of oxidative stress where selective ( R )-methionine sulfoxide formation on M69 of biphenyl hydrolase-like protein leads to hydrolase inhibition and amplification of proteome N -homocysteinylation modifications. This work introduces a platform for characterizing sites of asymmetric methionine oxidation and the functional consequences concomitant with an individual chiral single-atom modification.