Large sets of data need to be compacted for classification and extraction of information regarding structural changes of aminoacid units in specific sequences of proteins. The screen is constructed by opposite sides of the virtual tetrahedron built by the six distances between four centers and provides coordinates for a two-dimensional square plot. As alternative e.g. to Ramachandran diagrams based on angles, it may offer greater accuracy and sensitivity. The screen was initially employed to peroxides and persulfides, to monitor the distances relevant to chirality changing processes and successively to show some electric and kinetic properties. The smallest chiral aminoacid, alanine, was therefore chosen for the basic illustration presented here. A virtual tetrahedron is built by the six distances between four centers of the aminoacid skeleton: they do not necessarily coincide with bonds, so a computer program permits their calculation from tabulations of experimental and theoretical data. Here, the screen is applied to treat significant geometrical features of alanine as affected by adjacent aminoacids in peptide chains, as available on protein databases. In this exemplary presentation applications of screen plots are limited to biochemistry: elsewhere have been shown useful in other areas, such as spin networks and the kinematics of a four-bar mechanism.
Screens Displaying Structural Properties of Aminoacids in Polypeptide Chains: Alanine as a Case Study
Caglioti C.;Lombardi A.;Palazzetti F.
;Aquilanti V.
2019
Abstract
Large sets of data need to be compacted for classification and extraction of information regarding structural changes of aminoacid units in specific sequences of proteins. The screen is constructed by opposite sides of the virtual tetrahedron built by the six distances between four centers and provides coordinates for a two-dimensional square plot. As alternative e.g. to Ramachandran diagrams based on angles, it may offer greater accuracy and sensitivity. The screen was initially employed to peroxides and persulfides, to monitor the distances relevant to chirality changing processes and successively to show some electric and kinetic properties. The smallest chiral aminoacid, alanine, was therefore chosen for the basic illustration presented here. A virtual tetrahedron is built by the six distances between four centers of the aminoacid skeleton: they do not necessarily coincide with bonds, so a computer program permits their calculation from tabulations of experimental and theoretical data. Here, the screen is applied to treat significant geometrical features of alanine as affected by adjacent aminoacids in peptide chains, as available on protein databases. In this exemplary presentation applications of screen plots are limited to biochemistry: elsewhere have been shown useful in other areas, such as spin networks and the kinematics of a four-bar mechanism.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
