Mass Spectrometric Amino Acid Sequencing of Short and Mid-Sized Peptides in a ESI-o-TOF System as an Alternative to MS/MS. II: Selective Fragmentation of Dansylated Peptides with Predominant Formation of b-Ions

2019 ◽  
Vol 45 (1) ◽  
pp. 9-17
Author(s):  
I. V. Nazimov ◽  
R. A. Bublyaev
Keyword(s):  
Amino Acid ◽  
Mass Spectrometric ◽  
Predominant Formation ◽  
Amino Acid Sequencing

Integration of Biomolecular Interaction Analysis and Mass Spectrometric Amino Acid Sequencing

2000 ◽  
Vol 28 (5) ◽  
pp. A262-A262
Author(s):  
T. Natsume ◽  
H. Nakayama ◽  
O. Jansson ◽  
T. Isobe ◽  
K. Takio ◽  
...  
Keyword(s):  
Amino Acid ◽  
Interaction Analysis ◽  
Mass Spectrometric ◽  
Amino Acid Sequencing ◽  
Biomolecular Interaction ◽  
Biomolecular Interaction Analysis

Combination of Biomolecular Interaction Analysis and Mass Spectrometric Amino Acid Sequencing

2000 ◽  
Vol 72 (17) ◽  
pp. 4193-4198 ◽  
Author(s):  
Tohru Natsume ◽  
Hiroshi Nakayama ◽  
Östen Jansson ◽  
Toshiaki Isobe ◽  
Koji Takio ◽  
...  
Keyword(s):  
Amino Acid ◽  
Interaction Analysis ◽  
Mass Spectrometric ◽  
Amino Acid Sequencing ◽  
Biomolecular Interaction ◽  
Biomolecular Interaction Analysis

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.

Structural and functional studies on C4b-binding protein, a regulatory component of the human complement system

1985 ◽  
Vol 5 (10-11) ◽  
pp. 855-865 ◽  
Author(s):  
L. Ping Chung ◽  
Kenneth B. M. Reid
Keyword(s):  
Amino Acid ◽  
Binding Protein ◽  
Protein A ◽  
Limited Proteolysis ◽  
Binding Activity ◽  
Amino Acid Sequencing ◽  
Functional Studies ◽  
Before And After ◽  
Cofactor Activity ◽  
Long Chain

The binding and cofactor activities of C4b-binding protein were examined before and after limited proteolysis by pepsin, trypsin and chymotrypsin. The major fragments generated were characterized by amino acid sequencing, thus establishing the precise points of limited proteolysis. These studies allow a tentative assignment of the cofactor activity site to the residues 177–322 of the 549 amino acid long chain of C4b-binding protein but indicated that residues in the region 332–395 are important in the binding activity.

Sign in / Sign up

Export Citation Format

Share Document