scholarly journals The primary structure of proteins: Principles and practices for the determination of amino acid sequence (Schroeder, Walter)

1970 ◽  
Vol 47 (4) ◽  
pp. A310
Author(s):  
Charles L. Borders
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Structure Of Proteins

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.

scholarly journals Primary structure of hemoglobins from trout(Salmo irideus). Partial determination of amino acid sequence of Hb trout IV

FEBS Letters ◽  
1976 ◽  
Vol 64 (1) ◽  
pp. 76-80 ◽  
Author(s):  
F. Bossa ◽  
D. Barra ◽  
M. Coletta ◽  
F. Martini ◽  
A. Liverzani ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure

Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

2020 ◽  
Author(s):  
Michele Larocca
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Theoretical Approach ◽  
Polypeptide Chain ◽  
Hydrophobic Effect ◽  
Side Chain ◽  
Dihedral Angles ◽  
Mechanical Forces ◽  
Specific Chemical

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>

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