Successful amphiphiles as the key to crystallization of membrane proteins: Bridging theory and practice

Publication date: Available online 10 November 2018Source: Biochimica et Biophysica Acta (BBA) - General SubjectsAuthor(s): Joscha Breibeck, Annette RompelAbstractBackgroundMembrane proteins constitute a major group of proteins and are of great significance as pharmaceutical targets, but underrepresented in the Protein Data Bank. Particular reasons are their low expression yields and the constant need for cautious and diligent handling in a sufficiently stable hydrophobic environment substituting for the native membrane. When it comes to protein crystallization, such an environment is often established by detergents.Scope of reviewIn this review, 475 unique membrane protein X-ray structures from the online data bank “Membrane proteins of known 3D structure” are presented with a focus on the detergents essential for protein crystallization. By systematic analysis of the most successful compounds, including current trends in amphiphile development, we provide general insights for selection and design of detergents for membrane protein crystallization.Major conclusionsThe most successful detergents share common features, giving rise to favorable protein interactions. The hydrophile-lipophile balance concept of well-balanced hydrophilic and hydrophobic detergent portions is still the key to successful protein crystallization. Although a single detergent compound is sufficient in most cases, sometimes a suitable mixture of detergents has to be found to alter the resulting prot...
Source: Biochimica et Biophysica Acta (BBA) General Subjects - Category: Biochemistry Source Type: research