Water determines the structure and dynamics of proteins
MC Bellissent-Funel, A Hassanali, M Havenith… - Chemical …, 2016 - ACS Publications
Water is an essential participant in the stability, structure, dynamics, and function of proteins
and other biomolecules. Thermodynamically, changes in the aqueous environment affect …
and other biomolecules. Thermodynamically, changes in the aqueous environment affect …
High-pressure chemical biology and biotechnology
JL Silva, AC Oliveira, TCRG Vieira… - Chemical …, 2014 - ACS Publications
In his memorable book published in 1949, The Physics of High Pressure, 1 Bridgman states
that “it is a well-known result of thermodynamics that a substance is only completely …
that “it is a well-known result of thermodynamics that a substance is only completely …
Principles and practical applications of structure-based vaccine design
PO Byrne, JS McLellan - Current opinion in immunology, 2022 - Elsevier
Highlights•Summary of the basic principles of structure-based vaccine design.•Review of
recent advances (the years 2019–2021) in structure-based vaccine design.•Preview of …
recent advances (the years 2019–2021) in structure-based vaccine design.•Preview of …
Lessons from pressure denaturation of proteins
Although it is now relatively well understood how sequence defines and impacts global
protein stability in specific structural contexts, the question of how sequence modulates the …
protein stability in specific structural contexts, the question of how sequence modulates the …
[HTML][HTML] Modulation of allosteric coupling by mutations: from protein dynamics and packing to altered native ensembles and function
AN Naganathan - Current opinion in structural biology, 2019 - Elsevier
Highlights•Mutational effects are consistently felt beyond the first shell of
interactions.•Mutations modulate the dynamics and chemical shifts of distal …
interactions.•Mutations modulate the dynamics and chemical shifts of distal …
A general mechanism for the propagation of mutational effects in proteins
Mutations in the hydrophobic interior of proteins are generally thought to weaken the
interactions only in their immediate neighborhood. This forms the basis of protein …
interactions only in their immediate neighborhood. This forms the basis of protein …
Monitoring protein folding through high pressure NMR spectroscopy
High-pressure is a well-known perturbation method used to destabilize globular proteins. It
is perfectly reversible, which is essential for a proper thermodynamic characterization of a …
is perfectly reversible, which is essential for a proper thermodynamic characterization of a …
Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy
The time required to fold proteins usually increases significantly under conditions of high
pressure. Taking advantage of this general property of proteins, we combined P-jump …
pressure. Taking advantage of this general property of proteins, we combined P-jump …
Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology
Pressure and temperature are the two fundamental variables of thermodynamics.
Temperature and chemical perturbation are central experimental tools for the exploration of …
Temperature and chemical perturbation are central experimental tools for the exploration of …
A universal pattern in the percolation and dissipation of protein structural perturbations
N Rajasekaran, A Sekhar… - The journal of physical …, 2017 - ACS Publications
Understanding the extent to which information is transmitted through the intramolecular
interaction network of proteins upon a perturbation, that is, an allosteric effect, has long …
interaction network of proteins upon a perturbation, that is, an allosteric effect, has long …