An example of a peptide family that we have shown to form highly organized antiparallel b-sheets in membranes. See Medline Citation. In the laboratory we are using this class of molecules to study the fundamental principles of sheet formation in membranes. 
For example we are using differential scanning calorimetry to study the thermodynamics of sheet formation and we are using x-ray crystallography to study the atomic level interactions that give rise to sheet formation in membranes. We expect this information to be crucial in our membrane design and engineering projects.

These peptides bind to membranes as monomeric random coils, and then assemble into multimeric antiparallel b-sheets there. Unlike integral membrane proteins, these protein-like oligomers can fold and unfold reversibly along the pathway shown here. In the laboratory we take advantage of this property to study the fundamental principles of sheet formation in membranes.