Protein α-helices are ubiquitous secondary structural elements, seldom considered to be
stable without tertiary contacts. However, amino acid sequences in proteins that are based …

A relatively unknown protein structure motif forms stable isolated single α-helices, termed
ER/K α-helices, in a wide variety of proteins and has been shown to be essential for the …

Structural transitions are important for the stability and function of proteins, but these
phenomena are poorly understood. An extensive analysis of Protein Data Bank entries …

The α-helix is a ubiquitous secondary structural element that is almost exclusively observed
in proteins when stabilized by tertiary or quaternary interactions. However, beginning with …

Formation of α-helices is a fundamental process in protein folding and assembly. By
studying helix formation in molecular simulations of a series of alanine-based peptides, we …

In an effort to quantify the importance of hydrogen bonding and α-helix formation to protein
stability, a capping box motif was introduced into the small phosphocarrier protein HPr …

The noncovalent forces that stabilize protein structures are not fully understood. One way to
address this is to study equilibria between unfolded states and α-helices in peptides …

Arginine is a stabilizing element in both thermophilic and low molecular weight proteins.
Similarly Lys+→ Arg+ substitutions increase the helix content of designed helical peptides …

N3 is the third position from the N terminus in the α‐helix with helical backbone dihedral
angles. All 20 amino acids have been placed in the N3 position of a synthetic helical peptide …

Using a combination of ultraviolet circular dichroism, temperature-jump transient-infrared
spectroscopy, and molecular dynamics simulations, we investigate the effect of salt bridges …