Repozytorium
Wyszukaj
Kolekcje
Inne
His-rich sequences- is plagiarism from nature a good idea?
Autorzy
Rok wydania
2013
Czasopismo
Numer woluminu
37
Strony
58-70
DOI
10.1039/C2NJ40558J
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
In chemistry, nature-inspired solutions are often the most trivial and effective ones. Histidine rich sequences are used commercially in immobilized metal affinity chromatography (IMAC) as molecular ‘anchors’ that bind to a metal ion (usually nickel), immobilized by chelation with nitrilotriacetic acid (NTA) bound to a solid support. The typical (His)6 tag, present at the C- or N-terminus of a protein which is meant to be purified, has been successfully used for decades. Consecutive histidines are the common denominator for both His-tags used in molecular biology and for quite remote biological phenomena – polyhistidine sequences are found in some bacterial chaperones, in Zn2+ transporters, prion proteins, in histidine-rich glycoproteins (HRG), which posses a massive amount of functions, in some snake venoms and antimicrobial peptides. This work debates on two questions – first, why were such sequences chosen by nature to exist in some parts of specific, sometimes evolutionally remote proteins, and second, are we right about choosing the polyhistidine motif as the strongest metal binder?
Adres publiczny
http://dx.doi.org/10.1039/C2NJ40558J