Mass spectrometric studies of peptides. V. Determination of amino acid sequences in peptide mixtures by mass spectrometry

1973 ◽  
Vol 95 (10) ◽  
pp. 3369-3375 ◽  
Author(s):  
Hans Kaspar. Wipf ◽  
Philip. Irving ◽  
Malcolm. McCamish ◽  
Rengachari. Venkataraghavan ◽  
F. W. McLafferty
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Mass Spectrometric ◽  
Amino Acid Sequences ◽  
Peptide Mixtures

ChemInform Abstract: MASS SPECTROMETRIC STUDIES OF PEPTIDES PART 5, DETERMINATION OF AMINO ACID SEQUENCES IN PEPTIDE MIXTURES BY MASS SPECTROMETRYC

1973 ◽  
Vol 4 (30) ◽  
pp. no-no
Author(s):  
HANS-KASPAR WIPF ◽  
PHILIP IRVING ◽  
MALCOLM MCCAMISH ◽  
RENGACHARI VENKATARAGHAVAN ◽  
F. W. MCLAFFERTY
Keyword(s):  
Amino Acid ◽  
Mass Spectrometric ◽  
Amino Acid Sequences ◽  
Peptide Mixtures

Resolution of a protein sequence ambiguity by X-ray crystallographic and mass spectrometric methods

1992 ◽  
Vol 25 (2) ◽  
pp. 205-210 ◽  
Author(s):  
L. J. Keefe ◽  
E. E. Lattman ◽  
C. Wolkow ◽  
A. Woods ◽  
M. Chevrier ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Electron Density ◽  
Mass Spectrometric ◽  
Amino Acid Sequences ◽  
Data Matrix ◽  
Protein Crystal ◽  
Insertion Mutant ◽  
Laser Desorption Mass Spectrometry ◽  
X Ray

Ambiguities in amino acid sequences are a potential problem in X-ray crystallographic studies of proteins. Amino acid side chains often cannot be reliably identified from the electron density. Many protein crystal structures that are now being solved are simple variants of a known wild-type structure. Thus, cloning artifacts or other untoward events can readily lead to cases in which the proposed sequence is not correct. An example is presented showing that mass spectrometry provides an excellent tool for analyzing suspected errors. The X-ray crystal structure of an insertion mutant of Staphylococcal nuclease has been solved to 1.67 Å resolution and refined to a crystallographic R value of 0.170 [Keefe & Lattman (1992). In preparation]. A single residue has been inserted in the C-terminal α helix. The inserted amino acid was believed to be an alanine residue, but the final electron density maps strongly indicated that a glycine had been inserted instead. To confirm the observations from the X-ray data, matrix-assisted laser desorption mass spectrometry was employed to verify the glycine insertion. This mass spectrometric technique has sufficient mass accuracy to detect the methyl group that distinguishes glycine from alanine and can be extended to the more common situation in which crystallographic measurements suggest a problem with the sequence, but cannot pinpoint its location or nature.

scholarly journals Determination of amino acid sequences in peptides by mass spectrometry. Desulfurization of sulfur-containing peptides

FEBS Letters ◽  
1970 ◽  
Vol 8 (4) ◽  
pp. 207-209 ◽  
Author(s):  
R. Toubiana ◽  
J.E.G. Barnett ◽  
E. Sach ◽  
B.C. Das ◽  
E. Lederer
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Sulfur Containing

Determination of amino acid sequences in oligopeptides by mass spectrometry. II. The structure of peptidolipin NA

1965 ◽  
Vol 6 (18) ◽  
pp. 1331-1336 ◽  
Author(s):  
M. Barber ◽  
W.A. Wolstenholme ◽  
M. Guinand ◽  
G. Michel ◽  
B.C. Das ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequences

scholarly journals Mass Spectrometric Studies of Peptides. III.1Automated Determination of Amino Acid Sequences

1966 ◽  
Vol 88 (23) ◽  
pp. 5593-5597 ◽  
Author(s):  
Martin Senn ◽  
R. Venkataraghavan ◽  
F. W. McLafferty
Keyword(s):  
Amino Acid ◽  
Mass Spectrometric ◽  
Amino Acid Sequences

Determination of Amino Acid Sequences in Oligopeptides by Mass Spectrometry. IV. Synthetic N-Acyl Oligopeptide Methyl Esters*

Biochemistry ◽  
1965 ◽  
Vol 4 (10) ◽  
pp. 2254-2260 ◽  
Author(s):  
E. Bricas ◽  
J. van Heijenoort ◽  
M. Barber ◽  
W. A. Wolstenholme ◽  
B. C. Das ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Methyl Esters ◽  
Amino Acid Sequences

scholarly journals Determination of the sequences of protein-derived peptides and peptide mixtures by mass spectrometry

1971 ◽  
Vol 125 (1) ◽  
pp. 189-201 ◽  
Author(s):  
Howard R. Morris ◽  
Dudley H. Williams ◽  
Richard P. Ambler
Keyword(s):  
Mass Spectrometry ◽  
Prior Knowledge ◽  
Gel Filtration ◽  
Mass Spectrometric ◽  
Peptide Mixture ◽  
Peptide Mixtures ◽  
New Strategy ◽  
First Time ◽  
Resolution Mass

Micro-quantities of protein-derived peptides have been converted into N-acetylated permethyl derivatives, and their sequences determined by low-resolution mass spectrometry without prior knowledge of their amino acid compositions or lengths. A new strategy is suggested for the mass spectrometric sequencing of oligopeptides or proteins, involving gel filtration of protein hydrolysates and subsequent sequence analysis of peptide mixtures. Finally, results are given that demonstrate for the first time the use of mass spectrometry for the analysis of a protein-derived peptide mixture, again without prior knowledge of the protein or components within the mixture.

scholarly journals Mass-spectrometric determination of the amino acid sequences in peptides isolated from protein silk fibroin of Bombyx mori

1969 ◽  
Vol 114 (4) ◽  
pp. 695-702 ◽  
Author(s):  
A J Geddes ◽  
G N Graham ◽  
H R Morris ◽  
F. Lucas ◽  
M. Barber ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bombyx Mori ◽  
Silk Fibroin ◽  
Protein Hydrolysate ◽  
Exchange Chromatography ◽  
Mass Spectrometric ◽  
Amino Acid Sequences ◽  
Peptide Component ◽  
First Time

Several peptides were isolated from the protein silk fibroin of Bombyx mori by means of ion-exchange chromatography of a chymotryptic digest. The sequences of three of the peptides, Gly-Ala-Gly-Tyr, Gly-Val-Gly-Tyr and Gly-Ala-Gly-Ala-Gly-Ala-Gly-Tyr, were known from previous chemical work, but the sequence of the fourth, Gly-Ala-Gly-Val-Gly-Ala-Gly-Tyr, was previously only partially known. The necessary volatility for mass-spectrometric examination of the peptides was achieved by permethylation of the N-acetyl-peptide methyl ester derivatives. From the mass spectra it was possible to confirm the known sequences and to establish that of the partially known one. In one instance it was possible to deduce from the same mass spectrum the sequence of a main peptide component and that of a small amount of contaminating peptide. These results demonstrate for the first time the use of mass spectrometry in the determination of the amino acid sequences in peptides from a protein hydrolysate.

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