Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments

► 2H NMR data from transmembrane peptides are analyzed considering explicit dynamics. ► Tilt angles are calculated in lipid system-peptides at different hydrophobic mismatch. ► The mismatch behavior is highly dependent on flanking residues of the peptides. ► The tilt of WW-flanked peptides follows a simple cosine rule. ► KK-flanked cases deviate from cosine dependence due to change of length with mismatch.