ABSTRACT
Evaluation of the intramolecular stability of proteins plays a key role in the comprehension of their biological behavior and mechanism of action. Small structural alterations such as mutations induced by single nucleotide polymorphism can impact biological activity and pharmacological modulation. Covid-19 mutations, that affect viral replication and the susceptibility to antibody neutralization, and the action of antiviral drugs, are just one example. In this work, the intramolecular stability of mutated proteins, like Spike glycoprotein and its complexes with the human target, is evaluated through hydropathic intramolecular energy scoring originally conceived by Abraham and Kellogg based on the "Extension of the fragment method to calculate amino acid zwitterion and side-chain partition coefficients" by Abraham and Leo in Proteins: Struct. Funct. Genet. 1987, 2:130 - 52. HINT is proposed as a fast and reliable tool for the stability evaluation of any mutated system. This work has been written in honor of Prof. Donald J. Abraham (1936-2021).
Subject(s)
Oncogene Proteins , Spike Glycoprotein, Coronavirus , Humans , Oncogene Proteins/chemistry , Spike Glycoprotein, Coronavirus/chemistryABSTRACT
The rapid spread of COVID-19 made it necessary to quickly collect and share viral genomic sequences, sometimes making quantity prevail over the quality of information. Can research pay this price? Blockchain technology, based on the concept of a ledger that guarantees the authenticity and traceability of information, could be the best applicable solution.