Dear all:
Before I get delued with mail about my spelling skills, I would like to
apologize and confess to all of you that I have always scored a grade of
zero in dictation in French (my first lanuage) and the other languages I've
learned (English,Hebrew,Spanish and Arabic). Have a good Science week.
Amina
Amina S. Woods, Ph.D.
NIDA Intramural Program, NIH
5500 Nathan Schock Drive
Baltimore, MD 21224
Tel: 410-550-1507
Fax: 410-550-2971
e-mail: awoods@intra.nida.nih.gov
-----Original Message-----
From: neil brew [mailto:neil.brew@bbsrc.ac.uk]
Sent: Monday, April 17, 2000 4:15 AM
To: 'Amina S. Woods'
Subject: RE: MALDI: Protein dimmer
Surely you mean a dimer?
-----Original Message-----
From: Amina S. Woods [mailto:awoods@jhmi.edu]
Sent: 15 April 2000 17:16
To: Recipients of ABRF List
Subject: RE: MALDI: Protein dimmer
I do a lot of work at pH of 5-7 to study non-covalent interaction by
MALDI (Enzyme-Substrate complexes, DNA-peptide etc...). So I have to use
matrices with pH in the range of 5-7. In those cases I do see more dimmer
formation than usual even at low concentrations of compound deposited.
Usually if I look at the same sample using matrices at pH less than 2.0
these dimmers are absent.
I do believe that these dimmers are usually two molecules trapped
together. I have also unpublished data using basic matrices showing 5
isomers (MH+) as well as the MH2+.
If you are interested in non-covalent interaction I'll refer you to my
papers and others on the subject. I think the best paper to read is Terry
Farmar's review in the Journal of Mass Spectrometry. I think it was
published in 1998. Akos Vertes and John Callahan published in 1995, and
Louis Pannell also published in 1995 on non-covalent interaction seen by
MALDI
Amina S. Woods, Ph.D.
NIDA Intramural Program, NIH
5500 Nathan Schock Drive
Baltimore, MD 21224
Tel: 410-550-1507(office)
Tel:410-550-5168 (lab)
Fax: 410-550-2971
e-mail: awoods@intra.nida.nih.gov
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