A grand challenge in the field of structural biology is to design and engineer proteins that
exhibit targeted functions. Although much success on this front has been achieved, design …

Reverse turns are a major class of protein secondary structure; they represent sites of chain
reversal and thus sites where the globular character of a protein is created. It has been …

The classification of protein folds is necessarily based on the structural elements that
distinguish domains. Classification of protein domains consists of two problems: the partition …

β-Turns are common conformations that enable proteins to adopt globular structures, and
their formation is often rate limiting for folding. β-Turn mimics, molecules that replace the i+ 1 …

Interactions between proteins and carbohydrates are ubiquitous in biology. Therefore,
understanding the factors that determine their affinity and selectivity are correspondingly …

All-atom molecular dynamics (MD) simulations on increasingly powerful computers have
been combined with experiments to characterize protein folding in detail over wider time …

Most rotamer libraries are generated from subsets of the PDB and do not fully represent the
conformational scope of protein side chains. Previous attempts to rectify this sparse …

The stabilities of 66 sequence variants of the human Pin1 WW domain have been
determined by equilibrium thermal denaturation experiments. All 34 residues composing the …

Asparagine glycosylation is one of the most common and important post-translational
modifications of proteins in eukaryotic cells. N-Glycosylation occurs when a triantennary …

N‐glycosylation can increase the rate of protein folding, enhance thermodynamic stability,
and slow protein unfolding; however, the molecular basis for these effects is incompletely …