Cupane, Antonio

Schirò, Giorgio

Proteins, the nano-machines of living systems, are highly dynamic molecules. The time-scale of functionally relevant motions spans over a very broad range, from femtoseconds to several seconds. In particular, the pico- to nanoseconds

region is characterized by side-chain and backbone anharmonic fluctuations that are responsible for many biological tasks like ligand binding, substrate recognition and enzymatic activity. Neutron scattering on hydrated protein powders reveals two main activations of anharmonic dynamics, characterized by different onset temperature and amplitude. Here we review our work on synthetic polypeptides, native proteins, and single amino acids to identify the physical origin of the two onsets—one involving water-independent local dynamics of methyl groups and, to a minor extent, of aromatic side-chains, and the other one, known as “protein dynamical transition”, concerning large scale functional protein fluctuations, most likely induced by a crossover in the structure and dynamics of hydration water connected with the second critical point hypothesis

Schirò, G.

Cupane, A.

Scientific Open-access Literature Archive and Repository

English

Anharmonic activations in proteins and peptide model systems

and their connection with supercooled water thermodynamics

Proteins, the nano-machines of living systems, are highly dynamic
molecules. The time-scale of functionally relevant motions spans over a very broad
range, from femtoseconds to several seconds. In particular, the pico- to nanoseconds
region is characterized by side-chain and backbone anharmonic fluctuations that are
responsible for many biological tasks like ligand binding, substrate recognition and
enzymatic activity. Neutron scattering on hydrated protein powders reveals two
main activations of anharmonic dynamics, characterized by different onset temperature
and amplitude. Here we review our work on synthetic polypeptides, native
proteins, and single amino acids to identify the physical origin of the two onsets
—one involving water-independent local dynamics of methyl groups and, to a minor
extent, of aromatic side-chains, and the other one, known as “protein dynamical
transition”, concerning large scale functional protein fluctuations, most likely induced
by a crossover in the structure and dynamics of hydration water connected
with the second critical point hypothesis

Schirò G

Cupane A

Archivio istituzionale della ricerca - Università di Palermo

Anharmonic activations in proteins and peptide model systems
and their connection with supercooled water thermodynamics

International audience— Proteins, the nano-machines of living systems, are highly dynamic molecules. The timescale of functionally relevant motions spans over a very broad range, from femtoseconds to several seconds. In particular, the pico-to nanoseconds region is characterized by side-chain and backbone anharmonic fluctuations that are responsible for many biological tasks like ligand binding, substrate recognition and enzymatic activity. Neutron scattering on hydrated protein powders reveals two main activations of anharmonic dynamics, characterized by different onset temperature and amplitude. Here we review our work on synthetic polypeptides, native proteins, and single amino acids to identify the physical origin of the two onsets —one involving water-independent local dynamics of methyl groups and, to a minor extent, of aromatic side-chains, and the other one, known as " protein dynamical transition " , concerning large scale functional protein fluctuations, most likely induced by a crossover in the structure and dynamics of hydration water connected with the second critical point hypothesis

Hal-Diderot

Anharmonic activations in proteins and peptide model systems and their connection with supercooled water thermodynamics

International audienceProteins, the nano-machines of living systems, are highly dynamic molecules. The timescale of functionally relevant motions spans over a very broad range, from femtoseconds to several seconds. In particular, the pico-to nanoseconds region is characterized by side-chain and backbone anharmonic fluctuations that are responsible for many biological tasks like ligand binding, substrate recognition and enzymatic activity. Neutron scattering on hydrated protein powders reveals two main activations of anharmonic dynamics, characterized by different onset temperature and amplitude. Here we review our work on synthetic polypeptides, native proteins, and single amino acids to identify the physical origin of the two onsets —one involving water-independent local dynamics of methyl groups and, to a minor extent, of aromatic side-chains, and the other one, known as " protein dynamical transition " , concerning large scale functional protein fluctuations, most likely induced by a crossover in the structure and dynamics of hydration water connected with the second critical point hypothesis

Hal - Université Grenoble Alpes

HAL Descartes

HAL-CEA

https://iris.unipa.it/bitstream/10447/267059/1/2016_Schir%c3%b2%26Cupane_Il%20Nuovo%20Cimento%20C%2039%2c%20305%2c%202016.pdf

Anharmonic activations in proteins and peptide model systems and their connection with supercooled water termodynamics

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