helixdistorting

Helixdistorting describes perturbations of helical regions in macromolecules, including protein alpha helices, coiled coils, and nucleic acid helices, in which the regular geometry of the helix is perturbed. Distortions can range from subtle changes in twist or rise to pronounced bends, kinks, unwinding, or torsional strain, and they may alter stability and function of the macromolecule.

Causes of helixdistorting include substitutions that introduce helix-breaking residues such as proline, bulky side chains that create steric clashes, and alterations that shift backbone dihedral angles. Ligand binding, metal coordination, and post-translational modifications can also distort helices, as can environmental factors such as pH, temperature, and ionic strength.

In proteins, distortions can modulate folding, stability, and interactions with other molecules, and may contribute to allosteric regulation or activation of enzymatic sites. In nucleic acids, helixdistorting can affect base pairing, helix pitch, and recognition by proteins or enzymes, influencing replication, transcription, or RNA catalysis.

Detection and analysis rely on structural and spectroscopic techniques such as X-ray crystallography, nuclear magnetic resonance, cryo-electron microscopy, circular dichroism, and computational modeling, which quantify changes in dihedral angles, helix tilt, and bending, and relate them to functional outcomes.