Chapter 1
Allostery: The Rebound of Proteins
Alessandro Finazzi Agro ` and Giampiero Mei
Abstract
The discovery of hemoglobin allosteric properties is briefly summarized and contextualized in the frame of
the main biochemical revelations that characterized the first half of the XX century. In particular, the
historical background of DNA, RNA, and protein structure research is recalled and the new role that
protein-protein interaction may have on allosteric regulation is discussed.
Key words Myoglobin, Hemoglobin, Allosteric effect, Oligomerization
The history of Biochemistry in the past century can be jokingly, but
even not so much, due to pertinacity and pride of the respective
supporters, described as a fight for supremacy among proteins,
DNA and RNAs.
No doubt that the first half of twentieth century was dominated
by the biochemistry of proteins, especially those endowed with
enzymatic or other functionally well understandable functions.
The first and most famous among this class was, and is, hemoglobin, due to two remarkable and useful properties: our connatural
fascination (or aversion) for blood and the abundance and relative
easiness of its purification. In fact, hemoglobin was the first protein
to be purified and crystallized more than 150 years ago [1]. From
thence and for the following hundred years, proteins were the main
character on the biochemistry stage. Not by chance, their collective
name, proteins, comes indeed from the Greek word πρoτειoν (proteion, primary) [2]. Another important ability of proteins was
afterwards discovered: their role as organic catalysts soon denominated to enzymes (again a Greek-derived word: ενζυμoν, enzumon ¼ in leaven) [3]. As a matter of fact, already for thousands
of years the ability of yeast to convert organic matter into human’s
more desirable foods (beer, leavened bread, wine) was known and
exploited.
The elemental chemistry, amino acid composition, primary
(amino acids sequence), secondary, tertiary, and quaternary
Luisa Di Paola and Alessandro Giuliani (eds.), Allostery: Methods and Protocols, Methods in Molecular Biology, vol. 2253,
https://doi.org/10.1007/978-1-0716-1154-8_1, © Springer Science+Business Media, LLC, part of Springer Nature 2021
1
Allostery: The Rebound of Proteins
Alessandro Finazzi Agro ` and Giampiero Mei
Abstract
The discovery of hemoglobin allosteric properties is briefly summarized and contextualized in the frame of
the main biochemical revelations that characterized the first half of the XX century. In particular, the
historical background of DNA, RNA, and protein structure research is recalled and the new role that
protein-protein interaction may have on allosteric regulation is discussed.
Key words Myoglobin, Hemoglobin, Allosteric effect, Oligomerization
The history of Biochemistry in the past century can be jokingly, but
even not so much, due to pertinacity and pride of the respective
supporters, described as a fight for supremacy among proteins,
DNA and RNAs.
No doubt that the first half of twentieth century was dominated
by the biochemistry of proteins, especially those endowed with
enzymatic or other functionally well understandable functions.
The first and most famous among this class was, and is, hemoglobin, due to two remarkable and useful properties: our connatural
fascination (or aversion) for blood and the abundance and relative
easiness of its purification. In fact, hemoglobin was the first protein
to be purified and crystallized more than 150 years ago [1]. From
thence and for the following hundred years, proteins were the main
character on the biochemistry stage. Not by chance, their collective
name, proteins, comes indeed from the Greek word πρoτειoν (proteion, primary) [2]. Another important ability of proteins was
afterwards discovered: their role as organic catalysts soon denominated to enzymes (again a Greek-derived word: ενζυμoν, enzumon ¼ in leaven) [3]. As a matter of fact, already for thousands
of years the ability of yeast to convert organic matter into human’s
more desirable foods (beer, leavened bread, wine) was known and
exploited.
The elemental chemistry, amino acid composition, primary
(amino acids sequence), secondary, tertiary, and quaternary
Luisa Di Paola and Alessandro Giuliani (eds.), Allostery: Methods and Protocols, Methods in Molecular Biology, vol. 2253,
https://doi.org/10.1007/978-1-0716-1154-8_1, © Springer Science+Business Media, LLC, part of Springer Nature 2021
1