Raphael Alhadeff
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Raphael Alhadeff has a total of 4 co-authors. Here are the top co-authors by number of shared publications:
- Arieh Warshel
Department of Chemistry University of Southern California Los Angeles California USA
1 shared publication Chen Bai
Department of Chemistry, University of Southern California, Los Angeles, CA 90089
1 shared publicationMikolaj Feliks
Department of Chemistry, University of Southern California, Los Angeles, CA 90089
1 shared publicationMyungjin Lee
Department of Chemistry, University of Southern California, Los Angeles, CA 90089
1 shared publication
Latest Publications
- 25 September 2018
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 115 (41) , 10321-10326
On the control of the proton current in the voltage-gated proton channel Hv1
Significance: Voltage activation of proton transport is an important mechanism that plays a key role in fundamental biological processes, yet the detailed control of such processes is far from clear. Here we investigate the voltage-activated proton channel Hv1 to explore the structure/function basis of its activation by combining empirical valence bond and electrostatic calculations. Our study provides a detailed description of the exquisite use of an ionizable aspartic acid residue and arginine residues in controlling the crucial selectivity of the proton transport through the channel. This type of mechanism is likely to have implications for the action of other related systems.
- 25 September 2018
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 115 (41) , 10321-10326
On the control of the proton current in the voltage-gated proton channel Hv1
Significance: Voltage activation of proton transport is an important mechanism that plays a key role in fundamental biological processes, yet the detailed control of such processes is far from clear. Here we investigate the voltage-activated proton channel Hv1 to explore the structure/function basis of its activation by combining empirical valence bond and electrostatic calculations. Our study provides a detailed description of the exquisite use of an ionizable aspartic acid residue and arginine residues in controlling the crucial selectivity of the proton transport through the channel. This type of mechanism is likely to have implications for the action of other related systems.