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Related Concept Videos

Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
Phase Transitions: Melting and Freezing02:39

Phase Transitions: Melting and Freezing

Heating a crystalline solid increases the average energy of its atoms, molecules, or ions, and the solid gets hotter. At some point, the added energy becomes large enough to partially overcome the forces holding the molecules or ions of the solid in their fixed positions, and the solid begins the process of transitioning to the liquid state or melting. At this point, the temperature of the solid stops rising, despite the continual input of heat, and it remains constant until all of the solid is...
Entropy and Solvation02:05

Entropy and Solvation

The process of surrounding a solute with solvent is called solvation. It involves evenly distributing the solute within the solvent. The rule of thumb for determining a solvent for a given compound is that like dissolves like. A good solvent has molecular characteristics similar to those of the compound to be dissolved. For example, polar solutions dissolve polar solutes, and apolar solvents dissolve apolar solutes. A polar solvent is a solvent that has a high dielectric constant (ϵ ≥ 15); an...
DNA Isolation01:34

DNA Isolation

DNA from cells is required for many biotechnology and research applications, such as molecular cloning. To remove and purify DNA from cells, researchers use various methods of DNA extraction. While the specifics of different protocols may vary, some general concepts underlie the process of DNA extraction.
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
Recrystallization: Solid–Solution Equilibria01:10

Recrystallization: Solid–Solution Equilibria

Recrystallization is a purification technique used to separate impurities from solid compounds. In this technique, no chemical reactions occur. Instead, it exploits physical properties only, specifically, the solubility differences between the desired compound and impurities, either at a single temperature or at different temperatures, and under other selected conditions. The solid-solution equilibrium (solubility equilibrium) of each component in the solution represents a binary phase...

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Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

Protein cold denaturation as seen from the solvent.

Monika Davidovic1, Carlos Mattea, Johan Qvist

  • 1Department of Biophysical Chemistry, Center for Molecular Protein Science, Lund University, SE-22100 Lund, Sweden.

Journal of the American Chemical Society
|January 1, 2009
PubMed
Summary

Cold denaturation of globular proteins was investigated using water-(17)O spin relaxation. Only destabilized apomyoglobin cold denatured, challenging common assumptions about protein-water interactions and cold denaturation mechanisms.

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Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
08:13

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Area of Science:

  • Biophysics
  • Protein dynamics
  • Thermodynamics

Background:

  • Globular proteins have a temperature of maximum stability, unlike most ordered systems.
  • Cold denaturation, or structure disruption by cooling, is typically linked to hydrophobic forces.
  • Experimental investigation of hydration changes during cold denaturation is lacking.

Purpose of the Study:

  • To experimentally monitor hydration dynamics of proteins at low temperatures.
  • To investigate cold denaturation phenomena in various globular proteins.
  • To understand the role of protein-water interactions in cold denaturation.

Main Methods:

  • Water-(17)O spin relaxation was used to study hydration dynamics.
  • Proteins (BPTI, ubiquitin, apomyoglobin, beta-lactoglobulin) were studied in aqueous solution.
  • Solutions were contained in picoliter emulsion droplets to prevent ice formation down to -35°C.

Main Results:

  • Only destabilized apomyoglobin exhibited cold denaturation.
  • Ubiquitin remained stable down to -32°C; beta-lactoglobulin was unstable below -5°C but kinetically trapped.
  • Cold-denatured states were compact and solvent-penetrated, not fully unfolded, challenging analogies with nonpolar molecule solubility.

Conclusions:

  • Cold denaturation is protein-specific and influenced by stability and hydration.
  • The observed cold-denatured states suggest solvent penetration rather than complete unfolding.
  • Reported cold denaturation in some systems may be due to low water content, not temperature alone.