Alternative to conventional structural diagrams that plot dihedral angles of aminoacids in the protein chains, the proposed screen representation is based on significant distances in the aminoacid unit. Here, we report the case of alanine, the simplest chiral aminoacid, both isolated and participating in about fifty peptidic chains, of length included between 43 and 2238 aminoacid units. We present comparison with the most stable conformer in the isolated form (NH2-CH-CH3-COOH), in order to find possible effects in bond lengths due to aminoacid substituents. We have also found that serine is the aminoacid most frequently connected to alanine. Screen points of alanine, when bounded to serine, are displayed and highlighted in order to evidence how this aminoacid, exemplary for the substituent groups, affects the alanine structure.

Screen representation of structural properties of alanine in polypeptide chains

Caglioti C.
;
Palazzetti F.;Lombardi A.;Aquilanti V.
2019

Abstract

Alternative to conventional structural diagrams that plot dihedral angles of aminoacids in the protein chains, the proposed screen representation is based on significant distances in the aminoacid unit. Here, we report the case of alanine, the simplest chiral aminoacid, both isolated and participating in about fifty peptidic chains, of length included between 43 and 2238 aminoacid units. We present comparison with the most stable conformer in the isolated form (NH2-CH-CH3-COOH), in order to find possible effects in bond lengths due to aminoacid substituents. We have also found that serine is the aminoacid most frequently connected to alanine. Screen points of alanine, when bounded to serine, are displayed and highlighted in order to evidence how this aminoacid, exemplary for the substituent groups, affects the alanine structure.
978-073541933-9
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11391/1463006
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