Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Solution scattering of neutrons and x-rays can provide direct information on local interactions of importance for biomolecular folding and structure. Here, neutron scattering experiments are combined with molecular-dynamics simulation to interpret the scattering signal of a series of dipeptides with varying degrees of hydrophobicity (GlyAla, GlyPro, and AlaPro) in concentrated aqueous solution (1:20 solute/water ratio) in which the peptides form large segregates (up to 50-60 amino acids). Two main results are found: 1), the shift to lower Q of the so-called water-ring peak (Q ≈ 2 Å(-1)) arises mainly from an overlap of water-peptide and peptide-peptide correlations in the region of 1.3 <Q< 2 Å(-1), rather than from a shift of the water signal induced by the presence of the clusters; and 2), in the low-Q region (Q ≈ 0.6 Å(-1)) a positive peak is observed originating from both the solute-solute correlations and changes in the water structure induced by the formation of the clusters. In particular, the water molecules are found to be more connected than in the bulk with hydrogen-bonding directions tangential to the exposed hydrophobic surfaces, and this effect increases with increasing peptide hydrophobicity. This work demonstrates that important information on the (hydrophobic) hydration of biomolecules can be obtained in the very-small-angle region.

Original publication

DOI

10.1016/j.bpj.2012.08.010

Type

Journal article

Journal

Biophys J

Publication Date

03/10/2012

Volume

103

Pages

1518 - 1524

Keywords

Dipeptides, Hydrophobic and Hydrophilic Interactions, Molecular Dynamics Simulation, Neutron Diffraction, Protein Conformation, Scattering, Small Angle, Time Factors, Water