Specific interactions between amino acid side chains — a partial molar volume study

1988 ◽  
Vol 66 (3) ◽  
pp. 487-490 ◽  
Author(s):  
Mandapati V. R. Rao ◽  
Mahalakshmi Atreyi ◽  
Moganty R. Rajeswari

Partial molar volumes of the following mixtures, [Formula: see text](mix) were determined in water at 20 °C: (1) glutamic acid: glycine; (2) arginine:glycine; (3) arginine:glutamic acid; (4) arginine: aspartic acid; (5) lysine:glutamic acid, and (6) lysine: aspartic acid. Partial molar volumes of the mixtures calculated using [Formula: see text] of various ionic species of the amino acids agreed with the experimental values for systems 1 and 2, but were less than the experimental values for systems 3 to 6. The positive deviations, [Formula: see text] (mix), of the experimental values from the calculated values are discussed in terms of "specific interactions" between ionogenic side chains. The extent of interaction is greater in systems containing aspartic acid and/or arginine.

1984 ◽  
Vol 88 (14) ◽  
pp. 3129-3131 ◽  
Author(s):  
M. V. R. Rao ◽  
M. Atreyi ◽  
M. R. Rajeswari

ChemInform ◽  
2008 ◽  
Vol 39 (11) ◽  
Author(s):  
Stefania Capone ◽  
Silvana Pedatella ◽  
Annalisa Guaragna ◽  
Mauro De Nisco ◽  
Giovanni Palumbo

Molecules ◽  
2021 ◽  
Vol 26 (3) ◽  
pp. 712
Author(s):  
Piotr Minkiewicz ◽  
Małgorzata Darewicz ◽  
Anna Iwaniak ◽  
Marta Turło

Phosphorylation represents one of the most important modifications of amino acids, peptides, and proteins. By modifying the latter, it is useful in improving the functional properties of foods. Although all these substances are broadly annotated in internet databases, there is no unified code for their annotation. The present publication aims to describe a simple code for the annotation of phosphopeptide sequences. The proposed code describes the location of phosphate residues in amino acid side chains (including new rules of atom numbering in amino acids) and the diversity of phosphate residues (e.g., di- and triphosphate residues and phosphate amidation). This article also includes translating the proposed biological code into SMILES, being the most commonly used chemical code. Finally, it discusses possible errors associated with applying the proposed code and in the resulting SMILES representations of phosphopeptides. The proposed code can be extended to describe other modifications in the future.


2017 ◽  
Vol 15 (45) ◽  
pp. 9685-9695 ◽  
Author(s):  
H. Mukherjee ◽  
J. Debreczeni ◽  
J. Breed ◽  
S. Tentarelli ◽  
B. Aquila ◽  
...  

Profiling the reactivity and stability of SVI–F warheads towards nucleophilic amino acids for the development of biochemical probe compounds.


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