Biology under extreme conditions

Heremans, Karel

doi:10.1080/08957950310001635828

Cited by 10 publications

(4 citation statements)

References 61 publications

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“…Moreover, high pressure can induce unfolding of protein in a different way from thermal denaturation . The pressure studies have considerably increased in the past decade. ,− …”

Section: Pressure and Temperature Unfolding Of Proteinsmentioning

confidence: 99%

Water Determines the Structure and Dynamics of Proteins

et al. 2016

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Water is an essential participant in the stability, structure, dynamics, and function of proteins and other biomolecules. Thermodynamically, changes in the aqueous environment affect the stability of biomolecules. Structurally, water participates chemically in the catalytic function of proteins and nucleic acids and physically in the collapse of the protein chain during folding through hydrophobic collapse and mediates binding through the hydrogen bond in complex formation. Water is a partner that slaves the dynamics of proteins, and water interaction with proteins affect their dynamics. Here we provide a review of the experimental and computational advances over the past decade in understanding the role of water in the dynamics, structure, and function of proteins. We focus on the combination of X-ray and neutron crystallography, NMR, terahertz spectroscopy, mass spectroscopy, thermodynamics, and computer simulations to reveal how water assist proteins in their function. The recent advances in computer simulations and the enhanced sensitivity of experimental tools promise major advances in the understanding of protein dynamics, and water surely will be a protagonist.

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“…Moreover, high pressure can induce unfolding of protein in a different way from thermal denaturation . The pressure studies have considerably increased in the past decade. ,− …”

Section: Pressure and Temperature Unfolding Of Proteinsmentioning

confidence: 99%

Water Determines the Structure and Dynamics of Proteins

et al. 2016

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“…The mechanistic aspects underlying this phenomenon, called pressure-induced thermostabilization, are still elusive. Hei and Clark [43] suggested that the stabilization is correlated with the hydrophobicity of the protein, whereas Heremans [44] suggested a link with aggregation. Here, we have shown that pressure stabilizes myoglobin against temperatureinduced denaturation and concomitant aggregation.…”

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confidence: 99%

Extending the Pressure–Temperature State Diagram of Myoglobin

Meersman

Smeller

Heremans

2005

Helvetica Chimica Acta

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Dedicated to Professor AndreÂ E. Merbach on the occasion of his 65th birthdayThe pressure ± temperature (P,T) diagram of proteins proposed by Hawley concerns the equilibrium between native and denatured forms. However, the importance of protein aggregation is increasingly recognized, and it has been suggested that certain aggregated states represent alternative folds of the polypeptide chain. Here, we present a P,T-diagram for myoglobin in which we include the aggregated state and suggest to call it a P,T-state diagram, as not all boundaries are true equilibrium transitions. We observe by Fourier transform infrared spectroscopy that increasing temperature causes the protein to aggregate, but that a subsequent further temperature increase results in the dissociation of this aggregate. Moreover, we observe that moderate pressures stabilize myoglobin against thermal denaturation. We hypothesize that this effect originates from the volume changes associated with the aggregation transition.

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“…Although canonical DNA duplexes are stabilized by pressure, DNA-protein interactions may be perturbed due to changes in the electrostatic and hydrophobic interactions. Accordingly, pressure affects negatively all molecular reactions where DNA is involved, such as replication, transcription and recombination [28,29].…”

Section: Nucleic Acidsmentioning

confidence: 99%

High-pressure adaptation of extremophiles and biotechnological applications

Salvador-Castell

Oger

Peters

2020

Physiological and Biotechnological Aspects of Extremophiles

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During the last decades, high pressure has been an important physical parameter not only to study biomolecules, but also for its biotechnological applications. High pressure affects organism's ability to survive by altering most of cell's macromolecules. These effects can be used, for example, to inactivate microorganisms, enhance enzymatic reactions or to modulate cell activities. Moreover, some organisms are capable to growth under high pressures thanks to their adaptation at all cellular levels. Such adaptation confers a wide range of potentially interesting macromolecules still to be discovered. In this chapter, we firstly present the different effects of pressure on cells and the diverse strategies used to cope against this harsh environment. Secondly, we explored the pressure biotechnological applications on pressure-sensitive and adaptedpressure organisms.

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Biology under extreme conditions

Cited by 10 publications

References 61 publications

Water Determines the Structure and Dynamics of Proteins

Water Determines the Structure and Dynamics of Proteins

Extending the Pressure–Temperature State Diagram of Myoglobin

High-pressure adaptation of extremophiles and biotechnological applications

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