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

Computational simulations of protein folding can be used to interpret experimental folding
results, to design new folding experiments, and to test the effects of mutations and small …

The accurate modeling of energetic contributions to protein structure is a fundamental
challenge in computational approaches to protein analysis and design. We describe a …

Although a large percentage of eukaryotic proteomes consist of proteins with multiple
domains, not much is known about their assembly mechanism, especially those with …

Uncovering the structure and function of biomolecules is a fundamental goal in structural
biology. Membrane‐embedded transport proteins are ubiquitous in all kingdoms of life …

Although cooperativity is a well-established and general property of folding, our current
understanding of this feature in multidomain folding is still relatively limited. In fact, there are …

Although more than 75% of the proteome is composed of multidomain proteins, current
knowledge of protein folding is based primarily on studies of isolated domains. In this work …

Relating the native fold of a protein to its amino acid sequence remains a fundamental
problem in biology. While computer algorithms have demonstrated recently their prowess in …

Human acidic fibroblast growth factor (hFGF1) is an all beta-sheet protein that is involved in
the regulation of key cellular processes including cell proliferation and wound healing …

Investigating the evolution of structural features in modern multidomain proteins helps to
understand their immense diversity and functional versatility. The class of periplasmic …