Exploring the relevance of gas-phase structures to biology: cold ion spectroscopy of the decapeptide neurokinin A

Linking the intrinsic tertiary structures of biomolecules to their native geometries is a central prerequisite for making gas-phase studies directly relevant to biology. The isolation of molecules in the gas phase eliminates hydrophilic interactions with solvents, to some extent mimicking a hydrophobic environment. Intrinsic structures thereforemay resemble native ones for peptides that in vivo reside in a hydrophobic environment (e.g., binding pockets of receptors). In this study, we investigate doubly protonated neurokinin A (NKA) using IR-UV double resonance cold ion spectroscopy and find only five conformers of this decapeptide in the gas phase. In contrast, NMR data show that in aqueous solutions, NKA exhibits high conformational heterogeneity, which reduces to a few well-defined structures in hydrophobic micelles. Do the gas-phase structures of NKA resemble these native structures? The IR spectra reported here allow the validation of future structural calculations thatmay answer this question.


Published in:
Physical Chemistry Chemical Physics -Cambridge- Royal Society of Chemistry, 19, 5, 3468-3472
Year:
2017
Publisher:
Cambridge, Royal Society of Chemistry
ISSN:
1463-9076
Keywords:
Laboratories:




 Record created 2017-04-11, last modified 2018-03-17


Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)