The influence of the hydrogen-bond network on the structure and dynamics of the RAPRKKG heptapeptide and its mutants.

The structural behaviour of the RAPRKKG heptapeptide after individual or multiple mutations was inspected through molecular dynamics simulation. The nature of the mutations provided information on the flexibility of the heptapeptide and on how water molecules establish hydrogen bonds with it. The structural behaviour of the wild-type and the mutated structures were measured through the analysis of protein‒protein and protein‒solvent hydrogen bonds.

Temperature effect on the structure and conformational fluctuations in two zinc knuckles from the mouse mammary tumor virus.

Zinc fingers are small protein domains in which zinc plays a structural role, contributing to the stability of the zinc-peptide complex. Zinc fingers are structurally diverse and are present in proteins that perform a broad range of functions in various cellular processes, such as replication and repair, transcription and translation, metabolism and signaling, cell proliferation, and apoptosis. Zinc fingers typically function as interaction modules and bind to a wide variety of compounds, such as nucleic acids, proteins, and small molecules.

Effect of mutation on the stabilization energy of HIV-1 zinc fingers: a hybrid local self-consistent field/molecular mechanics investigation.

Metal-ligand interactions give rise to a wide variety of metal complexes with various physical properties and chemical behaviours and numerous practical applications. The ability of the zinc ion to enhance the structural stability of many proteins by electrostatic interactions or by co-ordination with surrounding amino acids makes it the most important metal ion found in biological systems. In this paper, we highlight the importance of non-covalent interaction established between a metal ion and its environment in stabilizing biomolecules.