Mechanical properties of amorphous and semi-crystalline semi-aromatic polyamides.

We investigate the mechanical properties of amorphous and semi-crystalline semi-aromatic polyamides, polyphthalamides (PPA). Three relaxation processes have been identified by DMTA which is consistent with literature for polyamide. PPA exhibit a brittle-to-ductile transition from a low impact strength to a high impact strength.

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin.

Neuroglobin (Ngb) is a globin present in the brain and retina of mammals. This hexacoordinated hemoprotein binds small diatomic molecules, albeit with lower affinity compared with other globins. Another distinctive feature of most mammalian Ngb is their ability to form an internal disulfide bridge that increases ligand affinity.

Frontier residues lining globin internal cavities present specific mechanical properties.

The internal cavity matrix of globins plays a key role in their biological function. Previous studies have already highlighted the plasticity of this inner network, which can fluctuate with the proteins breathing motion, and the importance of a few key residues for the regulation of ligand diffusion within the protein. In this Article, we combine all-atom molecular dynamics and coarse-grain Brownian dynamics to establish a complete mechanical landscape for six different globins chain (myoglobin, neuroglobin, cytoglobin, truncated hemoglobin, and chains α and β of hemoglobin).

Relating the diffusion of small ligands in human neuroglobin to its structural and mechanical properties.

Neuroglobin (Ngb), a recently discovered member of the globin family, is overexpressed in the brain tissues over oxygen deprivation. Unlike more classical globins, such as myoglobin and hemoglobin, it is characterized by a hexacoordinated heme, and its physiological role is still unknown, despite the numerous investigations made on the protein in recent years. Another important specific feature of human Ngb is the presence of two cysteine residues (Cys46 and Cys55), which are known to form an intramolecular disulfide bridge.