Peripheral membrane proteins are temporarily coupled to the surface of a membrane, penetrating into the lipid layer. In this work, it has been shown that the fraction of trans configurations of dihedral angles in hydrophobic chains of lipids decreases in the region of contact of peripheral membrane proteins with the membrane. This effect differs for different lipid chains and for dihedral angles at different distances from the beginning of a chain. A gosh configuration has a higher energy than a trans configuration. Consequently, the decrease in the fraction of trans configurations leads to an increase in the energy of the chain. The energy of chain conformations for the peripheral membrane protein considered in this work increases by ≈2 kJ/mol. A chain in chain conformations is involved in molecular mechanisms determining the elastic modulus of membranes. The energy stored in a conformation chain can be spent to the desorption of protein from the surface of the membrane and can be considered as a reason why the interaction of peripheral membrane proteins with the membrane is temporal.