<p>In each case the mutant structure refined by minimization is shown in cyan and the mutant structure where a 5A radius was refined by side-chain prediction is shown in brown. The mutation residue is shown in ball-and-stick. Panel A shows the C:Thr170Ala mutation in 1AHW along with nearby residues. Panels B and C show the C:Trp43Ala mutation in 1FCC. </p
Temperature-sensitive (TS) mutants are powerful tools to study gene function in vivo. These mutants ...
Point mutations are frequently used to explore the structure and/or function of proteins. The abilit...
<p>Based on an analysis of the current atomic model, we analyzed interactions between residues (midd...
<p>Colors for α chain, β chain, peptide, MHC, and mutant side chains from the crystal structure are ...
<p>Carbon atom, cyan; Nitrogen atom, blue; Oxygen atom, red. Mutation of CMG2 117 Glu to Gln is show...
<p>Dashes denote cases where the known mutation was not enriched in the predicted sequences using no...
<p>(A) Handle-region distance distributions for ecRNH WT (top) and V98A (bottom), illustrating the p...
Structures of point mutations (cyan) were generated using homology modeling and then aligned to know...
We assessed the ability of three widely used and freely available programs for side chain repacking ...
<p>Upon mutation, residues that result in a shift towards the “sharp” EPR spectrum are colored in ye...
<p>(A) Plot comparing the minimum and maximum simulated <i>T</i><sub>m</sub> values, for each residu...
<p><b>(A) Wild-type enzyme; (B) A269K/S187D mutant; (C) S187D/N188T mutant; D) A269K/S187D/N188T mut...
<p>Tested single residue mutations based on grouping system. Residues shown in red indicate mutation...
<p>The top row compares, from left to right, the double mutant to the wild type, the triple mutant t...
<p>Panel A shows the positions of mutations that yielded at least a 10% increase in specific activit...
Temperature-sensitive (TS) mutants are powerful tools to study gene function in vivo. These mutants ...
Point mutations are frequently used to explore the structure and/or function of proteins. The abilit...
<p>Based on an analysis of the current atomic model, we analyzed interactions between residues (midd...
<p>Colors for α chain, β chain, peptide, MHC, and mutant side chains from the crystal structure are ...
<p>Carbon atom, cyan; Nitrogen atom, blue; Oxygen atom, red. Mutation of CMG2 117 Glu to Gln is show...
<p>Dashes denote cases where the known mutation was not enriched in the predicted sequences using no...
<p>(A) Handle-region distance distributions for ecRNH WT (top) and V98A (bottom), illustrating the p...
Structures of point mutations (cyan) were generated using homology modeling and then aligned to know...
We assessed the ability of three widely used and freely available programs for side chain repacking ...
<p>Upon mutation, residues that result in a shift towards the “sharp” EPR spectrum are colored in ye...
<p>(A) Plot comparing the minimum and maximum simulated <i>T</i><sub>m</sub> values, for each residu...
<p><b>(A) Wild-type enzyme; (B) A269K/S187D mutant; (C) S187D/N188T mutant; D) A269K/S187D/N188T mut...
<p>Tested single residue mutations based on grouping system. Residues shown in red indicate mutation...
<p>The top row compares, from left to right, the double mutant to the wild type, the triple mutant t...
<p>Panel A shows the positions of mutations that yielded at least a 10% increase in specific activit...
Temperature-sensitive (TS) mutants are powerful tools to study gene function in vivo. These mutants ...
Point mutations are frequently used to explore the structure and/or function of proteins. The abilit...
<p>Based on an analysis of the current atomic model, we analyzed interactions between residues (midd...