(function(doc, html, url) {
var widget = doc.createElement("div");
widget.innerHTML = html;
var script = doc.currentScript; // e = a.currentScript;
if (!script) {
var scripts = doc.scripts;
for (var i = 0; i < scripts.length; ++i) {
script = scripts[i];
if (script.src && script.src.indexOf(url) != -1) break;
}
}
script.parentElement.replaceChild(widget, script);
}(document, '
Peptide Bonds Unveiled: Enhancing Protein Structure Understanding
What is it about?
High-resolution crystal structures reveal that peptide bonds in α-helices exhibit more enol-like characteristics than those in β-strands, including potential protonation of peptide oxygen atoms.
Why is it important?
This study underscores the unique insights provided by high-resolution protein crystallography, uncovering peptide bond properties that have been overlooked by traditional methods such as crystallography, NMR, and cryo-EM. It calls for a reconsideration of local restraints in structure refinements, shedding light on peptide bond dynamics crucial for protein function.