Detergents are amphiphilic compounds with crucial roles in the extraction, purification and stabilization of integral membrane proteins and in experimental studies of their structure and function. One technique that is highly dependent on detergents for solubilization of membrane proteins is solution-state nuclear magnetic resonance (NMR) spectroscopy, where detergent micelles often serve as the best membrane mimetic for achieving particle sizes that tumble fast enough to produce high-resolution/high-sensitivity spectra. The best quality NMR spectra use detergents with partial or complete deuteration, which eliminate interfering proton signals from the detergent itself and eliminate potential proton relaxation pathways and strong dipole-dipole interactions that contribute line broadening effects. Another technique for which deuterated detergents have been crucial to obtain structural information about membrane proteins in solution is small-angle neutron scattering (SANS). Use of a deuterated detergent exploits the intrinsic neutron scattering length difference between hydrogen and deuterium, such that detergent is matched-out in D2O and only signal from the membrane protein remains visible in the scattering profile, simplifying data analysis. We provide an updated review on the properties, chemical synthesis and applications of detergents that are commercially available and/or that have been synthesized with partial or complete deuteration, and that have been used in NMR or SANS studies on membrane proteins. Specifically, the detergents are sodium dodecyl sulphate (SDS), lauryldimethylamine-oxide (LDAO), n-octyl-β-D-glucoside (β-OG), n-dodecyl-β-D-maltoside (DDM) and fos-cholines including dodecylphosphocholine (DPC). We also consider effects of deuteration, detergent screening and guidelines for detergent selection.