title: Quantifying transient interactions between amide groups and the guanidinium cation.
abstract: We study the interaction of the guanidinium cation, a widely used protein denaturant, with amide groups, the common structural motif of proteins. Our results provide evidence for direct contact between guanidinium and ∼2 amide groups, but the interaction is transient and weaker than for other cations with high charge-density.
authors.affiliation: Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany. hunger@mpip-mainz.mpg.de.
authors.forename: V
authors.initials: V
authors.lastname: Balos
authors.affiliation: Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany. hunger@mpip-mainz.mpg.de.
authors.forename: M
authors.initials: M
authors.lastname: Bonn
authors.affiliation: Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany. hunger@mpip-mainz.mpg.de.
authors.forename: J
authors.initials: J
authors.lastname: Hunger
mesh_terms: D000081:Acetamides / Q000737:chemistry; D000577:Amides / Q000737:chemistry*; D002412:Cations; D019277:Entropy; D019791:Guanidine / Q000737:chemistry*; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D014867:Water / Q000737:chemistry
chemical_list: D000081:Acetamides; D000577:Amides; D002412:Cations; D011506:Proteins; D014867:Water; D019791:Guanidine; C018595:N-methylacetamide