Is absorbance at 205 nm not a possibility, Jack?
Casper Wilkens
Asst. Prof.
Structural Enzymology & Biorefining
DTU Bioengineering
Technical University of Denmark
[http://www.dtu.dk/%7E/media/DTU_Generelt/Andet/DTU_email_logo_01.gif]
Department of Biotechnology and Biomedicine
Søltofts Plads
Building 224
Room 028
2800 Kgs. Lyngby
[email protected]<mailto:[email protected]>
www.bioengineering.dtu.dk/<http://www.bioengineering.dtu.dk/>
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________________________________
Fra: CCP4 bulletin board <[email protected]> på vegne af Artem Evdokimov
<[email protected]>
Sendt: 19. februar 2022 02:12:50
Til: [email protected]
Emne: Re: [ccp4bb] Strategies for increasing Trp content of proteins
We have had success placing single trp on the outside of proteins, as weird as
it sounds it works pretty well. If your protein is easy to express you can try
a few choices.
If your protein is difficult to express, a fusion with a trp-positive domain or
with gfp may be a better option.
There are many other options but their application is best considered with more
information in hand
Artem
On Fri, Feb 18, 2022, 8:02 PM Tanner, John J.
<[email protected]<mailto:[email protected]>> wrote:
Dear CCP4BB,
We are working on a protein that has no Trp residues, which makes
chromatography challenging due to the low absorbance at 280 nm (Abs 0.1% =
0.104). Does anyone have experience using mutagenesis to increase the Trp
content of proteins?
Thanks,
Jack Tanner
--
John J. Tanner
Professor of Biochemistry and Chemistry
Associate Chair of Biochemistry
Department of Biochemistry
University of Missouri
117 Schweitzer Hall
503 S College Avenue
Columbia, MO 65211
Phone: 573-884-1280
Email: [email protected]<mailto:[email protected]>
https://cafnrfaculty.missouri.edu/tannerlab/
Lab: Schlundt Annex rooms 3,6,9, 203B, 203C
Office: Schlundt Annex 203A
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