Most H-NMR experiments with deuterated phospholipids demonstrate that the presence of proteins has little effect on either the order parameter of the lipids in the bilayer or the lipid dynamics, as measured by relaxation times. The overall view resulting from NMR experiments is 1) that the exchange rate between boundary and free lipids is rapid, (10 sec), 2) that the order parameters of the bound lipid are barely affected by being adjacent to proteins, 3) that the dynamics of the acyl chain reorientations are slowed only slightly in the frequency range of 10 sec, and 4) that the orientation and the dynamics of the polar headgroups are similarly unaffected in any substantial manner by being adjacent to transmembrane proteins. 13C-NMR spectrum also gives information on specific lipid-protein interactions of biomembranes 
Recent results using non labeled optical methods such as Dual Polarisation Interferometry which measure the birefringence(or order) within lipid bilayers have been used to show how peptide and protein interactions can influence bilayer order, specifically demonstrating the real time association to bilayer and critical peptide concentration after which the peptides penetrate and disrupt the bilayer order.