Editorial “High-pressure biophysical chemistry: Exploring the dynamical landscape of biomolecular systems by pressure perturbation”

2020 ◽  
Vol 258 ◽  
pp. 106328
Author(s):  
Roland Winter
Keyword(s):  
High Pressure ◽  
Pressure Perturbation ◽  
Biomolecular Systems ◽  
Biophysical Chemistry

Probing conformational and functional substates of calmodulin by high pressure FTIR spectroscopy: influence of Ca2+ binding and the hypervariable region of K-Ras4B

2016 ◽  
Vol 18 (43) ◽  
pp. 30020-30028 ◽  
Author(s):  
Nelli Erwin ◽  
Satyajit Patra ◽  
Roland Winter
Keyword(s):  
High Pressure ◽  
Ftir Spectroscopy ◽  
Target Recognition ◽  
Hypervariable Region ◽  
Pressure Perturbation ◽  
Conformational Substates

Using pressure perturbation, conformational substates of CaM could be uncovered that conceivably facilitate target recognition by exposing the required binding surfaces.

scholarly journals Biomolecular systems under pressure

2014 ◽  
Vol 70 (a1) ◽  
pp. C1188-C1188
Author(s):  
Andrzej Katrusiak ◽  
Michalina Aniola ◽  
Kamil Dziubek ◽  
Kinga Ostrowska ◽  
Ewa Patyk
Keyword(s):  
High Pressure ◽  
Double Helix ◽  
Building Blocks ◽  
Moderate Pressure ◽  
Molecular Architecture ◽  
Biomolecular Systems ◽  
Laboratory Equipment ◽  
Egg White Lysozyme ◽  
High Pressure Studies ◽  
Tetragonal Form

Biological systems are often regarded as the ultimate goal of all knowledge in this respect that they can provide the clue for understanding the origin of life and the means for improving the life conditions and healthcare. Hence the interest in high-pressure behavior of organic and biomolecular systems. Such simple organic systems were among the first structural studies at high pressure at all. They included chloroform by Roger Fourme in 1968 [1] and benzene by Piermarini et al. in 1969, still with the use of photographic technique. The efficient studies on bio-macromolecular crystals had to wait for several decades till synchrotron radiation became more accessible and Roger Fourme again stood in the avant-garde of these studies [2]. At the turn of centuries his innovations in the laboratory equipment and experimental setup let him exploring high-pressure conformations of proteins, viral capsids and the double-helix molecular architecture in nucleic acids. These directions of high-pressure studies are continued for simple and macromolecular systems of biological importance. Recently new surprising facts were revealed about the compression of urea, sucrose, and other organic compounds, as well as of macromolecular crystals. Sugars are the main energy carriers for animals as well as building blocks in the living tissue, they are also ideal models for studying pressure-induced changes of OH···O and CH···O interactions. Different types of transformations occur in compressed urea, the first organic compound synthesized in laboratory. Hen egg-white lysozyme was investigated at moderate pressure in a beryllium vessel and the compression of both tetragonal and orthorhombic modifications were measured to 1.0 GPa in a DAC; the high-pressure structure of the tetragonal form was determined and refined at still higher pressure by Fourme et al. [3] Can high pressure provide information about the remarkable polymorphism of lysozyme?

Quartz Ultraviolet Rydberg Transitions in Benzene Isomers

1979 ◽  
Vol 32 (12) ◽  
pp. 2579 ◽  
Author(s):  
PJ Harman ◽  
JE Kent ◽  
MF O'Dwyer ◽  
MH Smith
Keyword(s):  
High Pressure ◽  
Experimental Evidence ◽  
Absorption Spectra ◽  
Matrix Isolation ◽  
Valence Shell ◽  
Pressure Perturbation ◽  
The Matrix ◽  
Rydberg Transitions

Investigation of the matrix isolation and high-pressure perturbation spectra of the benzene isomers, benzvalene, Dewar benzene and fulvene, has shown conclusively that the structured regions in the absorption spectra of these molecules around 200 nm are due not to valence shell transitions but rather are Rydberg transitions to 3s type states. In the light of the experimental evidence reassignments of the spectra of each of these molecules have been proposed.

Exploring the temperature–pressure configurational landscape of biomolecules: from lipid membranes to proteins

2004 ◽  
Vol 363 (1827) ◽  
pp. 537-563 ◽  
Author(s):  
R. Winter ◽  
W. Dzwolak
Keyword(s):  
High Pressure ◽  
Lipid Membranes ◽  
Phase Behaviour ◽  
Pressure Jump ◽  
Spectroscopic Techniques ◽  
Biomolecular Systems ◽  
Time Resolved ◽  
Temperature And Pressure ◽  
Pressure Jump Relaxation ◽  
The Stability

Hydrostatic pressure has been used as a physical parameter for studying the stability and energetics of biomolecular systems, such as lipid mesophases and proteins, but also because high pressure is an important feature of certain natural membrane environments and because the high–pressure phase behaviour of biomolecules is of biotechnological interest. By using spectroscopic and scattering techniques, the temperature– and pressure–dependent structure and phase behaviour of lipid systems, differing in chain configuration, headgroup structure and concentration, and proteins have been studied and are discussed. A thermodynamic approach is presented for studying the stability of proteins as a function of both temperature and pressure. The results demonstrate that combined temperature–pressure dependent studies can help delineate the free–energy landscape of proteins and hence help elucidate which features and thermodynamic parameters are essential in determining the stability of the native conformational state of proteins. We also introduce pressure as a kinetic variable. Applying the pressure jump relaxation technique in combination with time–resolved synchrotron X–ray diffraction and spectroscopic techniques, the kinetics of un/refolding of proteins has been studied. Finally, recent advances in using pressure for studying misfolding and aggregation of proteins will be discussed.

scholarly journals A novel ER membrane protein Ehg1/May24 plays a critical role in maintaining multiple nutrient permeases in yeast under high-pressure perturbation

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Goyu Kurosaka ◽  
Satoshi Uemura ◽  
Takahiro Mochizuki ◽  
Yuri Kozaki ◽  
Akiko Hozumi ◽  
...  
Keyword(s):  
High Pressure ◽  
Yeast Species ◽  
Critical Role ◽  
Nutrient Transport ◽  
Deletion Mutants ◽  
Pressure Perturbation ◽  
Stabilizing Effect ◽  
The Stability ◽  
Growth Ability ◽  
Er Membrane

AbstractPreviously, we isolated 84 deletion mutants in Saccharomyces cerevisiae auxotrophic background that exhibited hypersensitive growth under high hydrostatic pressure and/or low temperature. Here, we observed that 24 deletion mutants were rescued by the introduction of four plasmids (LEU2, HIS3, LYS2, and URA3) together to grow at 25 MPa, thereby suggesting close links between the genes and nutrient uptake. Most of the highly ranked genes were poorly characterized, including MAY24/YPR153W. May24 appeared to be localized in the endoplasmic reticulum (ER) membrane. Therefore, we designated this gene as EHG (ER-associated high-pressure growth gene) 1. Deletion of EHG1 led to reduced nutrient transport rates and decreases in the nutrient permease levels at 25 MPa. These results suggest that Ehg1 is required for the stability and functionality of the permeases under high pressure. Ehg1 physically interacted with nutrient permeases Hip1, Bap2, and Fur4; however, alanine substitutions for Pro17, Phe19, and Pro20, which were highly conserved among Ehg1 homologues in various yeast species, eliminated interactions with the permeases as well as the high-pressure growth ability. By functioning as a novel chaperone that facilitated coping with high-pressure-induced perturbations, Ehg1 could exert a stabilizing effect on nutrient permeases when they are present in the ER.

High-pressure freezing of cells in suspension for low-voltage scanning electron microscopy (LVSEM)

1991 ◽  
Vol 49 ◽  
pp. 64-65
Author(s):  
Marek Malecki ◽  
James Pawley ◽  
Hans Ris
Keyword(s):  
Electron Microscopy ◽  
High Pressure ◽  
Low Voltage ◽  
Culture Media ◽  
Cell Structure ◽  
Freeze Substitution ◽  
Ice Crystal ◽  
High Pressure Freezing ◽  
Cell Culture Media ◽  
Voltage Scanning

The ultrastructure of cells suspended in physiological fluids or cell culture media can only be studied if the living processes are stopped while the cells remain in suspension. Attachment of living cells to carrier surfaces to facilitate further processing for electron microscopy produces a rapid reorganization of cell structure eradicating most traces of the structures present when the cells were in suspension. The structure of cells in suspension can be immobilized by either chemical fixation or, much faster, by rapid freezing (cryo-immobilization). The fixation speed is particularly important in studies of cell surface reorganization over time. High pressure freezing provides conditions where specimens up to 500μm thick can be frozen in milliseconds without ice crystal damage. This volume is sufficient for cells to remain in suspension until frozen. However, special procedures are needed to assure that the unattached cells are not lost during subsequent processing for LVSEM or HVEM using freeze-substitution or freeze drying. We recently developed such a procedure.

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