Inherent disordered proteins (IDP)

Inherent disordered proteins (IDP) is a kind of can't fold into three-dimensional structure of protein stability or orderly.Unlike folded proteins, the characteristics of the IDP is highly disordered, local mobility and high dynamic.Compared with has a clear three dimensional structure of protein, these characteristics give them completely different functional advantages.

In recent years, through the use of nuclear magnetic resonance (NMR) sequence specificity distribution, it was found that the intrinsic importance of disordered proteins (IDPs) in biology.IDPs now thought in the pathophysiology of health system and a variety of diseases have important biological significance.

Because of the lack of structure and high liquidity, the IDPs may be difficult.They can't use the traditional X-ray crystallography technique to characterize, and nuclear magnetic resonance (NMR) is the preferred tool.Nuclear magnetic resonance (NMR) has developed into in the structural biology research, including IDPs, protein dynamics of a powerful technology.Now, researchers can take advantage of new technology to overcome the allocation is not complete, chemical shift low dispersion and modification after translation cannot be detected.

Brooke is through the use of advanced nuclear magnetic resonance (NMR) solutions help clarify function structural biology research.New level GHz NMR technique for protein - to the structure of the ligand affinity and specificity of interaction between foundation for advanced study, including a better understanding of membrane protein structure characteristic, as well as protein folding and aggregation of the molecular mechanisms involved in.

1.2 GHz improvement of spectral resolution and sensitivity of nuclear magnetic resonance (NMR), has led the team to a more in-depth study on protein, a better understanding of amyloid accumulation of initial steps as well as the function and structure of the Tau protein, which is often associated with alzheimer's disease.