Hydrogen Bonding and Solvation of a Proline-Based Peptide by SR-UVRR

In polypeptide sequences, the amino acid proline (Pro) is considered to have a unique role in determining protein structure and folding. Multi-wavelength UV resonance Raman (UVRR) spectroscopy is a powerful method for investigating the hydrogen bonding in peptides and proteins containing Pro. 

The hydrogen bonding of water and water/salt mixtures around the proline-based tripeptide model GPG-NH2 is investigated here by Synchrotron UV Resonance Raman spectroscopy (SE-UVRR) to clarify the role of ion–peptide interactions in affecting the conformational stability of this peptide. The application of the SR-UVRR method to bioactive peptides containing X-Pro bonds could help in rationalizing the impact of salts as co-solutes on the trans–cis isomerization about the proline bond that is believed to be critical for the stability, dynamics and folding of proteins.
 

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Life, 11, 824, (2021) 
Ultima modifica il Mercoledì, 01 Settembre 2021 19:12