HIGH RESOLUTION ELECTROSPRAY MASS SPECTROMETRY WITH A MAGNETIC SECTOR INSTRUMENT: ACCURATE MASS MEASUREMENT AND PEPTIDE SEQUENCING

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Authors
  1. D'Agostino, P.A.
  2. Hancock, J.R.
  3. Provost, L.R.
  4. Semchuk, P.D.
  5. Hodges, R.S.
Corporate Authors
Defence Research Establishment Suffield, Ralston ALTA (CAN);Alberta Univ, Edmonton ALTA (CAN) Dept of Biochemistry
Abstract
The accurate molecular weights for a series of thirty-seven unknown synthetic peptides, used in research studies involving synthetic vaccines, antibacterial peptides or the de novo design of helical peptides and proteins, were determined with a magnetic sector instrument. All data were obtained with external calibration over a wide mass range during magnetic scanning. Errors between observed and theoretical monoisotopic molecular weights were typically in the 5 to 60 ppm range for the unknowns at section resolutions between 2500 and 9000 (10% valley). Isotopic clusters for charge states up to +10 were resolved through the use of high sector resolution. Collisional activated dissociation in the electrospray interface afforded production of product ions that enable either full or partial sequencing of most unknown peptides below 2000 Da. The complete primary sequence for one peptide was determined and the importance of high resolution was demonstrated by the differentiation of Lysine from Glutamine, two amino acides differing in residue mass by only 0.0364 Da. Two other peptides, with identical monoisotopic masses, but different primary sequences, were differentiated based on their CAD/MS data.
Report Number
DRES-622 —
Date of publication
01 Jan 1995
Number of Pages
37
DSTKIM No
95-01295
CANDIS No
151210
Format(s):
Hardcopy;Document Image stored on Optical Disk

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