The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …

Proteins provide much of the scaffolding for life, as well as undertaking a variety of essential
catalytic reactions. These characteristic functions have led us to presuppose that proteins …

Intrinsically disordered proteins (IDPs) are predicted to represent a significant fraction of the
human genome, and the development of meaningful molecular descriptions of these …

The biogenesis of integral outer-membrane proteins (OMPs) in Gram-negative bacteria
requires molecular chaperones that prevent the aggregation of OMP polypeptides in the …

The 70-kDa heat shock protein (Hsp70) family of chaperones bind cognate substrates to
perform a variety of different processes that are integral to cellular homeostasis. Although …

Summary α-Synuclein plays an important role in synaptic functions by interacting with
synaptic vesicle membrane, while its oligomers and fibrils are associated with several …

Disordered states of proteins include the biologically functional intrinsically disordered
proteins and the unfolded states of normally folded proteins. In recent years, ensemble …

Structural disorder of functional proteins under physiological conditions is widespread within
eukaryotic proteomes. The lack of stable tertiary and secondary structure offers a variety of …

Molecular chaperones are essential in aiding client proteins to fold into their native structure
and in maintaining cellular protein homeostasis. However, mechanistic aspects of …

Periplasmic binding proteins (PBPs) are a large family of molecular transporters that play a
key role in nutrient uptake and chemotaxis in Gram-negative bacteria. All PBPs have …