European Biophysics Journal

, Volume 37, Issue 5, pp 647–655 | Cite as

Water structure around dipeptides in aqueous solutions

  • Sylvia E. McLain
  • Alan K. Soper
  • Anthony Watts
Original Paper


The bulk water structure around small peptide fragments—glycyl-l-alanine, glycyl-l-proline and l-alanyl-l-proline—has been determined by a combination of neutron diffraction with isotopic substitution and empirical potential structural refinement techniques. The addition of each of the dipeptides to water gives rise to decreased water–water coordination in the surrounding water solvent. Additionally, both the Ow–Ow radial distribution functions and the water–water spatial density functions in all of the solutions indicate an electrostrictive effect in the second water coordination shell of the bulk water network. This effect is not observed in similar experiments on the amino acid l-proline alone in solution, which is one component of two of the peptides measured here.


Neutron diffraction Peptides in solution 



We thank the US-National Science foundation for fellowship monies for Sylvia McLain under award OISE-0404938 and Isabella Diadone (University of Heidelberg, Germany) for useful discussions.


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Copyright information

© EBSA 2008

Authors and Affiliations

  • Sylvia E. McLain
    • 1
  • Alan K. Soper
    • 2
  • Anthony Watts
    • 3
  1. 1.Neutron Scattering Sciences Division and Center for Molecular BiophysicsOak Ridge National LaboratoryOak RidgeUSA
  2. 2.ISIS FacilityRutherford Appleton LaboratoryDidcotUK
  3. 3.Biochemistry DepartmentUniversity of OxfordOxfordUK

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