The past several years have seen novel insights at the interface of protein biophysics and
evolution. The accepted paradigm that proteins can tolerate nearly any amino acid …

The relevance of protein stability for biological function and molecular evolution is widely
recognized. Protein stability, however, comes in two flavours: thermodynamic stability, which …

Local protein interactions (“molecular context” effects) dictate amino acid replacements and
can be described in terms of site-specific, energetic preferences for any different amino acid …

Understanding the determinants of protein stability remains one of protein science's greatest
challenges. There are still no computational solutions that calculate the stability effects of …

Consensus design, the selection of mutations based on the most common amino acid in
each position of a multiple sequence alignment, has proven to be an efficient way to …

It appears plausible that natural selection constrains, to some extent at least, the stability in
many natural proteins. If, during protein evolution, stability fluctuates within a comparatively …

We propose an application of molecular information theory to analyze the folding of single
domain proteins. We analyze results from various areas of protein science, such as …

Human proteins are vulnerable towards disease-associated single amino acid replacements
affecting protein stability and function. Interestingly, a few studies have shown that …

One selection pressure shaping sequence evolution is the requirement that a protein fold
with sufficient stability to perform its biological functions. We present a conceptual framework …

Biliverdin reductase (BVR) was characterized some 25 years ago as a unique dual-
cofactor/pH-dependent enzyme that catalyzes the reduction of biliverdin-IXa. Our knowledge …