One of the hallmark advances in our understanding of metalloprotein function is showcased
in our ability to design new, non-native, catalytically active protein scaffolds. This review …

The remarkable complexity of globular protein structures was first revealed about half a
century ago, when the crystal structure of myoglobin was determined at 2.4 Å. 1 In the …

X-ray crystallography has been applied to the structural analysis of a series of tetrapeptides
that were previously assessed for catalytic activity in an atroposelective bromination …

The quinazolinone and pyridol-pyrimidine classes of p38 MAP kinase inhibitors have a
previously unseen degree of specificity for p38 over other MAP kinases. Comparison of the …

Proteins are dynamic molecules and often undergo conformational change upon ligand
binding. It is widely accepted that flexible loop regions have a critical functional role in …

Proteins must move between different conformations of their native ensemble to perform
their functions. Crystal structures obtained from high-resolution X-ray diffraction data reflect …

The sequence GXXXXGKT/S, popularly known as Walker motif A, is widely believed to be
the site for binding nucleotides in many proteins. Examination of the crystal structures in the …

We report the development of a method to parameterize and predict the performance of
structurally flexible β-turn-containing peptide catalysts, using the atroposelective …

Photographs courtesy of Prof. P. Balaram, Indian Institute of Science. Nature has used the all-
α-polypeptide backbone of proteins to create a remarkable diversity of folded structures …

The crystal structure of 12 peptides containing the conformationally constrained 1-
(aminomethyl) cyclohexaneacetic acid, gabapentin (Gpn), are reported. In all the 39 Gpn …