Conformations of Myoglobin-Derived Peptides at the Air–Water Interface

The conformational
change exhibited by proteins at liquid interfaces,
such as the air–water and oil–water interfaces, has
long been of interest both for understanding protein structure outside
of native environments and for applications in areas including food
technology and pharmaceuticals. Using molecular simulation, this article
studies the conformations of two peptides derived from myoglobin,
for which the emulsification behavior has been studied. Both peptides
were found to readily adsorb onto the air–water interface,
with one of these (experimentally, the more effective stabilizer)
adopting a flat, extended conformation and the other peptide remaining
close to its solution conformation.