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 …

Myriad biological processes proceed through states that defy characterization by
conventional atomic-resolution structural biological methods. The invisibility of these …

The pathogenesis of Alzheimer's disease is characterized by the aggregation and fibrillation
of amyloid peptides Aβ1–40 and Aβ1–42 into amyloid plaques. Despite strong potential …

Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …

In this review, I discuss the various methods researchers use to unfold proteins in the lab in
order to understand protein folding both in vitro and in vivo. The four main techniques …

Recently, we reported that, in mice, hunger causes the autophagy-dependent release of a
protein called “acyl-CoA-binding protein” or “diazepam binding inhibitor”(ACBP/DBI) from …

The characterization of denatured states of proteins is challenging because the lack of
permanent structure in these states makes it difficult to apply to them standard methods of …

Research into the mechanisms by which proteins fold into their native structures has been
on-going since the work of Anfinsen in the 1960s. Since that time, the folding mechanisms of …

Binding of ligands is often crucial for function yet the effects of ligand binding on the
mechanical stability and energy landscape of proteins are incompletely understood. Here …

Rhodopseudomonas palustris cytochrome c′, a four-helix bundle, and the second ubiquitin-
associated domain, UBA (2), a three-helix bundle from the human homologue of yeast …