Variations in sensitivity to chlorine in Ecuador and US consumers: implications for community water systems.

Successful implementation of chlorination for disinfecting community water systems in developing countries faces obstacles, with rejection of chlorinous flavor as a significant factor. Determining consumers' abilities to accurately detect chlorine in treated water is important to identifying acceptable chlorination levels that are also effective for water disinfection. Chlorine detection sensitivity was tested in untrained Ecuadorian consumers with limited prior experience with chlorinated water and US consumers with extensive prior experience with chlorinated water.

Iron binding β-hairpin peptides.

Posttranslational modification of tyrosine to 3,4-dihydroxyphenylalanine (dopa) yields a unique functional group in biomolecular systems. Oxidation produces a quinone, which can undergo cross linking while deprotonation is well suited to metal binding. Mussels, tunicates and bacteria chelate iron and other metals with multiple dopa subunits.

pH-induced conformational change of the influenza M2 protein C-terminal domain.

The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy, we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We obtained residue-specific environmental parameters under both high- and low-pH conditions for nine consecutive C-terminal sites.

Determining the orientation of uniaxially rotating membrane proteins using unoriented samples: a 2H, 13C, AND 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle.

Membrane protein orientation has traditionally been determined by NMR using mechanically or magnetically aligned samples. Here we show a new NMR approach that abolishes the need for preparing macroscopically aligned membranes. When the protein undergoes fast uniaxial rotation around the bilayer normal, the 0 degrees -frequency of the motionally averaged powder spectrum is identical to the frequency of the aligned protein whose alignment axis is along the magnetic field.

Polar networks control oligomeric assembly in membranes.

Polar interactions have a profound influence on membrane stability and structure. A membrane-solubilized GCN4 peptide, MS-1, is used to study the impact of polar networks. Amide functionalities from amino acid side chains have been shown to promote peptide oligomerization, but lacked specificity.

Effect of halogenation on edge-face aromatic interactions in a beta-hairpin peptide: enhanced affinity with iodo-substituents.

[reaction: see text] In a model beta-hairpin peptide, we have found that the favorable interaction of cross-strand aromatic rings can be enhanced by up to 1 kcal mol(-1) with halogen substituents. It appears that the polarizability of the halogen atoms accounts for the increase in stability and that there is a direct interaction between the N-terminal phenylalanine and the halogen atom. Thermal denaturation studies indicate that the interaction is enthalpically driven with an associated entropic cost.

Investigation of the nature of the methionine-pi interaction in beta-hairpin peptide model systems.

There are frequent contacts between aromatic rings and sulfur atoms in proteins. However, it is unclear to what degree this putative interaction is stabilizing and what the nature of the interaction is. We have investigated the aryl-sulfur interaction by placing a methionine residue diagonal to an aromatic ring on the same face of a beta-hairpin, which places the methionine side chain in close proximity to the aryl side chain.

Comparison of C-H...pi and hydrophobic interactions in a beta-hairpin peptide: impact on stability and specificity.

We have examined the impact of C-H...

The geometry and efficacy of cation-pi interactions in a diagonal position of a designed beta-hairpin.

Cation-pi interactions are common in proteins, but their contribution to the stability and specificity of protein structure has not been well established. In this study, we examined the impact of cation-pi interactions in a diagonal position of a beta-hairpin peptide through comparison of the interaction of Phe or Trp with Lys or Arg. The diagonal interactions ranged from -0.

Simple cation-pi interaction between a phenyl ring and a protonated amine stabilizes an alpha-helix in water.

Cation-pi interactions have been proposed to be important contributors to protein structure and function. In particular, these interactions have been suggested to provide significant stability at the solvent-exposed surface of a protein. We have investigated the magnitude of cation-pi interactions between phenylalanine (Phe) and lysine (Lys), ornithine (Orn), and diaminobutanoic acid (Dab) in the context of an alpha-helix and have found that only the Phe.

Selective aromatic interactions in beta-hairpin peptides.

To probe the selectivity possible in hydrophobic clusters, we have compared the cross-strand interactions of phenylalanine (Phe) and cyclohexylalanine (Cha) in a beta-hairpin peptide. We have found a preference for self-association among the aromatic residues, which provides 0.55 kcal/mol in stability relative to Cha-Cha cross-strand pair.