The understanding of protein function is greatly enhanced by the availability of three dimensional structural information obtained by X- ray crystallography. Unfortunately the large, well-ordered three- dimensional crystals required for X-ray analyses have been difficult to produce for membrane proteins since they tend more naturally to form two- dimensional arrays. A further complicating factor in dealing with membrane proteins is the requirement for detergents to solubilize and stabilize the native structure. Although crystallization of membrane proteins is more of an art than a science as yet, it is clear that the structure and purity of the detergent are critical factors. In Phase II we will expand on the number of alkyl phosphocholines prepared in Phase I to include the cyclohexyl alkyl moietys in addition to others. Note that the some of the alkyl phosphocholines synthesized and evaluated were better than the available alkyl glucosides and maltosides.
Available detergents are not satisfactory in many cases. A great need exists for new, pure structurally defined detergents for purifying and analyzing membrane proteins. Anatrace plans to market these new detergents to the research community via its established distribution routes.
| Gorzelle, B M; Nagy, J K; Oxenoid, K et al. (1999) Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein. Biochemistry 38:16373-82 |
