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

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

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.

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.

A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form

Development ◽  
1999 ◽  
Vol 126 (18) ◽  
pp. 4077-4086 ◽  
Author(s):  
W. Hampe ◽  
J. Urny ◽  
I. Franke ◽  
S.A. Hoffmeister-Ullerich ◽  
D. Herrmann ◽  
...  
Keyword(s):  
Stem Cells ◽  
Amino Acid ◽  
Transmembrane Domain ◽  
Binding Protein ◽  
Amino Acid Sequences ◽  
Secreted Protein ◽  
Specific Antibodies ◽  
Head Activator ◽  
Carboxy Terminal

The neuropeptide head activator plays an important role for proliferation and determination of stem cells in hydra. By affinity chromatography a 200 kDa head-activator binding protein, HAB, was isolated from the multiheaded mutant of Chlorohydra viridissima. Partial amino acid sequences were used to clone the HAB cDNA which coded for a receptor with a unique alignment of extracellular modules, a transmembrane domain, and a short carboxy-terminal cytoplasmic tail. A mammalian HAB homologue with identical alignment of these modules is expressed early in brain development. Specific antibodies revealed the presence of HAB in hydra as a transmembrane receptor, but also as secreted protein, both capable of binding head activator. Secretion of HAB during regeneration and expression in regions of high determination potential hint at a role for HAB in regulating the concentration and range of action of head activator.

Determination of Factor Xa Activity by Means of Chromogenic Substrates Based on the Primary Structure of Prothrombin

1975 ◽  
Author(s):  
L. Aurell ◽  
A. Olausson ◽  
G. Claeson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Serine Proteases ◽  
Factor Xa ◽  
Amino Acid Sequences ◽  
Peptide Substrate ◽  
Chromogenic Substrates ◽  
Special Regard

Through the work of Magnusson and co-workers leading to the elucidation of the primary structure of prothrombin including the amino acid sequences around the two bonds split by factor Xa it has been possible to design a synthetic chromogenic peptide substrate. Bz-Ile-Glu-Gly-Arg-pNA, specifically intended for the determination of factor Xa. Furthermore, additional substrates have been synthezised with various alterations in the amino acid sequence. The activity of factor Xa and other serine proteases within the coagulation and fibrinolytic systems towards these substrates will be discussed with special regard to their possible use in coagulation studies.

The Influence of Dipeptide Composition on Protein Folding Rates

2011 ◽  
Vol 378-379 ◽  
pp. 157-160
Author(s):  
Jian Xiu Guo ◽  
Ni Ni Rao
Keyword(s):  
Protein Folding ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Dipeptide Composition ◽  
Coupling Effects ◽  
Jackknife Test ◽  
Folding Rates ◽  
Important Challenge ◽  
The Relationship

Understanding the relationship between amino acid sequences and folding rates of proteins is an important challenge in computational and molecular biology. All existing algorithms for predicting protein folding rates have never taken into account the sequence coupling effects. In this work, a novel algorithm was developed for predicting the protein folding rates from amino acid sequences. The prediction was achieved on the basis of dipeptide composition, in which the sequence coupling effects are explicitly included through a series of conditional probability elements. Based on a non-redundant dataset of 99 proteins, the proposed method was found to provide an excellent agreement between the predicted and experimental folding rates of proteins when evaluated with the jackknife test. The correlation coefficient was 87.7% and the standard error was 2.04, which indicated the important contribution from sequence coupling effects to the determination of protein folding rates.

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