Retention of histidine-containing peptides on a nickel affinity column.
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.
Kozlov
Igor A
IA
Illumina, Inc., San Diego, CA 92121, USA.
Kermani
Bahram G
BG
Melnyk
Peter C
PC
Barker
David L
DL
Zhao
Chanfeng
C
Hachmann
John P
JP
Lebl
Michal
M
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity / Q000295:instrumentation*; D006639:Histidine / Q000737:chemistry*; D008969:Molecular Sequence Data; D009532:Nickel; D010455:Peptides / Q000737:chemistry*
D010455:Peptides; D006639:Histidine; D009532:Nickel