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-liehavior 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.