Beta-aspartic acid (b-Asp) and gamma-glutamic acid (g-Glu) residues are amino acid residues in which the peptide bond is formed through the carboxylic acid group on the side chain rather than at the alpha carbon (normal). The form of aspartic acid (normal-Asp vs. b-Asp) in a peptide can greatly affect the activity of the peptide; likewise, the form of glutamic acid (normal-Glu vs. G-Glu) affects the peptide activity. We can identify the type of aspartic acid or glutamic acid linkage present by using analysis by MALDI-PSD of the TMPP-Ac-derivatives. The mass spectrum of the peptide containing a side chain-linked residue (b-Asp or g-Glu) had a b-type ion peak that was more intense than the corresponding b-type ion peak in the spectrum of the peptide containing the normal residue (Asp or Glu). Experiments with paired isomers of model peptides are being studied in an effort to establish useful protocols for identification of unknowns.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR000480-28S1
Application #
6258783
Study Section
Project Start
1997-06-01
Project End
1999-11-30
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
28
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Michigan State University
Department
Type
DUNS #
193247145
City
East Lansing
State
MI
Country
United States
Zip Code
48824
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Hosmane, R S; Hong, M (1997) How important is the N-3 sugar moiety in the tight-binding interaction of coformycin with adenosine deaminase? Biochem Biophys Res Commun 236:88-93
Lopez-Lara, I M; Orgambide, G; Dazzo, F B et al. (1993) Characterization and symbiotic importance of acidic extracellular polysaccharides of Rhizobium sp. strain GRH2 isolated from acacia nodules. J Bacteriol 175:2826-32
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