Unlike random heteropolymers, natural proteins fold into unique ordered structures.
Understanding how these are encoded in amino-acid sequences is complicated by …

The study of proteolysis lies at the heart of our understanding of biocatalysis, enzyme
evolution, and drug development. To understand the degree of natural variation in protease …

We present a model, based on symmetry and geometry, for proteins. Using elementary
ideas from mathematics and physics, we derive the geometries of discrete helices and …

This Perspective is intended to raise questions about the conventional interpretation of
protein folding. According to the conventional interpretation, developed over many decades …

Beta-hairpins are substructures found in proteins that can lend insight into more complex
systems. Furthermore, the folding of beta-hairpins is a valuable test case for benchmarking …

We have shown recently that the notion of poking pairwise interactions along a chain
provides a unifying framework for understanding the formation of both secondary and the …

Globular proteins adopt complex folds, composed of organized assemblies of α‐helix and β‐
sheet together with irregular regions that interconnect these scaffold elements. Here, we …

By using the composite vector with increment of diversity, position conservation scoring
function, and predictive secondary structures to express the information of sequence, a …

Loops connect regular secondary structures. In many instances, they are known to play
important biological roles. Analysis and prediction of loop conformations depend directly on …

Linear groups—polypeptide conformations based on a single repeating ϕ, ψ‐pair—are a
foundational concept in protein structure, yet how they are presented in textbooks is based …