V
Victoria A. Feher
Researcher at University of California, San Diego
Publications - 37
Citations - 3018
Victoria A. Feher is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Peptide sequence & Protein secondary structure. The author has an hindex of 24, co-authored 36 publications receiving 2608 citations. Previous affiliations of Victoria A. Feher include Scripps Research Institute & Scripps Health.
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Gaussian Accelerated Molecular Dynamics: Unconstrained Enhanced Sampling and Free Energy Calculation.
TL;DR: The free energy profiles obtained from reweighting of the GaMD simulations allow us to identify distinct low-energy states of the biomolecules and characterize the protein-folding and ligand-binding pathways quantitatively.
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Two-Component Signal Transduction in Bacillus subtilis: How One Organism Sees Its World
TL;DR: The sporulation initiation phosphorelay is a signal integration circuit that processes both positive and negative signals, which suggests that phosphorelays are used where a number of opposing signals must be interpreted by the signal transduction system.
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Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F.
Victoria A. Feher,John Cavanagh +1 more
TL;DR: This work uses a set of nuclear magnetic resonance 15N relaxation measurements to determine the relative timescales of Spo0F backbone fluctuations on the picosecond-to-millisecOND timescale and shows that regions having motion on the millisecond timescale correlate with residues and surfaces that are known to be critical for protein–protein interactions.
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Emerging Computational Methods for the Rational Discovery of Allosteric Drugs.
Jeffrey R. Wagner,Christopher T. Lee,Jacob D. Durrant,Robert D. Malmstrom,Victoria A. Feher,Rommie E. Amaro +5 more
TL;DR: Algorithms that predict allosteric sites based on sequence data and molecular dynamics simulations are reviewed, tools that assess the druggability of these pockets are described, and how Markov state models and topology analyses provide insight into the relationship between protein dynamics andallosteric drug binding are discussed.
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Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin.
TL;DR: The folding propensities of two peptides (Mb-G and Mb-H), corresponding to the G- and H-helix segments of the myoglobin sequence, are described and a novel method for assessing the distribution of helical populations based on the relative magnitudes of medium-range d alpha beta (i,i+3) NOE connectivities is estimated.