title: Selection of soluble protein expression constructs: the experimental determination of protein domain boundaries.
abstract: Proteins can contain multiple domains each of which is capable of possessing a separate independent function and three-dimensional structure. It is often useful to clone and express individual protein domains to study their biochemical properties and for structure determination. However, the annotated domain boundaries in databases such as Pfam or SMART are not always accurate. The present review summarizes various strategies for the experimental determination of protein domain boundaries.
authors.affiliation: Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK. md458@cam.ac.uk
authors.forename: Michael R
authors.initials: MR
authors.lastname: Dyson
mesh_terms: D000818:Animals; D019411:Clinical Laboratory Techniques; D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D017930:Genes, Reporter / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D020539:Sequence Analysis, Protein / Q000379:methods*; D012995:Solubility
chemical_list: D011506:Proteins; D011994:Recombinant Proteins