Selection of soluble protein expression constructs: the experimental determination of protein domain boundaries.
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.
Dyson
Michael R
MR
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK. md458@cam.ac.uk
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
D011506:Proteins; D011994:Recombinant Proteins