Can I read Study of the interactions between a proline‐rich protein and a flavan‐3‐ol by NMR: Residual structures in the natively unfolded protein provides anchorage points for the ligands on EtoBox?

Study of the interactions between a proline‐rich protein and a flavan‐3‐ol by NMR: Residual structures in the natively unfolded protein provides anchorage points for the ligands by Christine Pascal; Franck Paté; Véronique Cheynier; Marc‐André Delsuc is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Study of the interactions between a proline‐rich protein and a flavan‐3‐ol by NMR: Residual structures in the natively unfolded protein provides anchorage points for the ligands about?

## Abstract Astringency is one of the major organoleptic properties of food and beverages that are made from plants, such as tea, chocolate, beer, or red wine. This sensation is thought to be due to interactions between tannins and salivary proline‐rich proteins, which are natively unfolded proteins. A human salivary proline‐rich protein, namely IB‐5, was produced by the recombinant method. Its interactions with a model tannin, epigallocatechin gallate (EGCG), the major flavan‐3‐ol in green tea, were studied here. Circular dichroism experiments showed that IB‐5 presents residual structures (PPII helices) when the ionic strength is close to that in saliva. In the presence of these residual structures, IB‐5 undergoes an increase in structural content upon binding to EGCG. NMR data corroborated the presence of preformed structural elements within the protein prior to binding and a partial assignment was proposed, showing partial structuration. TOCSY experiments showed that amino acids that are involved in PPII helices are more likely to interact with EGCG than those in random coil regions, as if they were anchorage points for the ligand. The signal from IB‐5 in the DOSY NMR spectrum r

Who reads Study of the interactions between a proline‐rich protein and a flavan‐3‐ol by NMR: Residual structures in the natively unfolded protein provides anchorage points for the ligands?

Author

Christine Pascal; Franck Paté; Véronique Cheynier; Marc‐André Delsuc

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)