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Protein Flexibility Facilitates Quaternary Structure Assembly and Evolution

The flexibility of individual proteins aids their evolutionary recruitment into complexes with increasing numbers of distinct subunits.

Structural and evolutionary versatility in protein complexes with uneven stoichiometry

. Teichmann AuthorsSearch for Joseph A. Marsh in:Nature Research journals • PubMed • Google ScholarSearch for Holly A. Rees in:Nature Research journals • PubMed • Google ScholarSearch for Sebastian E. Ahnert ... authors analysed the results and wrote the paper. Competing interests The authors declare no competing financial interests. Corresponding author Correspondence to Joseph A. Marsh. Supplementary

Fast and Accurate Resonance Assignment of Small-to-Large Proteins by Combining Automated and Manual Approaches

The process of resonance assignment is fundamental to most NMR studies of protein structure and dynamics. Unfortunately, the manual assignment of residues is tedious and time-consuming, and can represent a significant bottleneck for further characterization. Furthermore, while automated approaches have been developed, they are often limited in their accuracy, particularly for...

How do proteins gain new domains?

A study of the contributions of different mechanisms of domain gain in animal proteins suggests that gene fusion is likely to be most frequent.

Characterization of disordered proteins with ENSEMBLE

Summary: ENSEMBLE is a computational approach for determining a set of conformations that represents the structural ensemble of a disordered protein based on input experimental data. The disordered protein can be an unfolded or intrinsically disordered state. Here, we introduce the latest version of the program, which has been enhanced to facilitate its general release and...