title: Retention of histidine-containing peptides on a nickel affinity column.
abstract: The retention of histidine-containing peptides in immobilized metal-affinity chromatography is studied using several hundred modeled peptides. Retention is driven primarily by the number of histidine residues; however, the amino acid composition in the immediate vicinity plays a significant role. Specifically, the arginine and tryptophan content has to be taken into consideration. During the course of this study, an alternative tag that can be used similarly to a polyhistidine tag is discovered.
authors.affiliation: Illumina, Inc., San Diego, CA 92121, USA.
authors.forename: Igor A
authors.initials: IA
authors.lastname: Kozlov
authors.forename: Bahram G
authors.initials: BG
authors.lastname: Kermani
authors.forename: Peter C
authors.initials: PC
authors.lastname: Melnyk
authors.forename: David L
authors.initials: DL
authors.lastname: Barker
authors.forename: Chanfeng
authors.initials: C
authors.lastname: Zhao
authors.forename: John P
authors.initials: JP
authors.lastname: Hachmann
authors.forename: Michal
authors.initials: M
authors.lastname: Lebl
mesh_terms: D000595:Amino Acid Sequence; D002846:Chromatography, Affinity / Q000295:instrumentation*; D006639:Histidine / Q000737:chemistry*; D008969:Molecular Sequence Data; D009532:Nickel; D010455:Peptides / Q000737:chemistry*
chemical_list: D010455:Peptides; D006639:Histidine; D009532:Nickel