Publisher Summary Turns are a fundamental class of polypeptide structure and are defined
as sites where the peptide chain reverses its overall direction. In the past 20 years, the …

During biosynthesis, a globular protein folds into a tight particle with an interior core that is
shielded from the surrounding solvent. The hydrophobic effect is thought to play a key role in …

Under physiological conditions, a protein undergoes a spontaneous disorder ⇌ order
transition called “folding.” The protein polymer is highly flexible when unfolded but adopts its …

The α helix, first proposed by Pauling and co-workers, is a hallmark of protein structure, and
much effort has been directed toward understanding which sequences can form helices. The …

Osmolytes are small organic compounds that affect protein stability and are ubiquitous in
living systems. In the equilibrium protein folding reaction, unfolded (U) ⇌ native (N), protecting …

The folding reactions of some small proteins show clear evidence of a hierarchic process,
whereas others, lacking detectable intermediates, do not. Nevertheless, we argue that both …

The protein loop, a novel category of nonregular secondary structure, is a segment of
contiguous polypeptide chain that traces a "loop-shaped" path in three-dimensional space; the …

A global census of the hydrogen bonds in 42 X-ray-elucidated proteins was taken and the
following demographic trends identified: (1) Most hydrogen bonds are local, ie between …

A sequence of seven alanine residues—too short to form an α-helix and whose side chains
do not interact with each other—is a particularly simple model for testing the common …

The literature abounds with arguments about whether a protein hydrogen bond is stabilizing
or destabilizing. Controversy also surrounds the hydro phobic effect. Long thought to be the …