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Related Concept Videos

Urea Cycle01:23

Urea Cycle

The urea cycle describes how liver cells convert ammonia to urea. Ammonia is a toxic waste product of protein catabolism. Land animals must convert ammonia into the less toxic urea which can be safely eliminated by the kidneys through urine. Marine animals excrete ammonia directly, and the surrounding water dilutes the ammonia to safe levels.
Structure of Amines01:19

Structure of Amines

The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’ carbon–carbon bond (154 pm). These aspects are illustrated in Figure...
Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Serum Studies: Renal Function Tests01:24

Serum Studies: Renal Function Tests

Renal function tests are crucial for assessing kidney health, monitoring disease progression, and evaluating the kidneys' efficiency in waste elimination, fluid balance, and electrolyte regulation. These tests offer critical insights into kidney function, even though routine measurements may appear normal until there is a significant decline in the glomerular filtration rate or GFR. Typically, signs of kidney impairment only become evident when the GFR falls to about 50% of its normal level.
Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...

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Related Experiment Video

Updated: Jun 12, 2026

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Urea interactions with protein groups: a volumetric study.

Soyoung Lee1, Yuen Lai Shek, Tigran V Chalikian

  • 1Leslie Dan Faculty of Pharmacy, Department of Pharmaceutical Sciences, University of Toronto, 144 College Street, Toronto, Ontario, Canada M5S 3M2.

Biopolymers
|June 22, 2010
PubMed
Summary

Urea denatures proteins by interacting with various protein groups. This study quantifies urea

Area of Science:

  • Biophysical Chemistry
  • Chemical Thermodynamics
  • Protein Denaturation

Background:

  • Urea is a known protein denaturant, but the precise molecular mechanisms of its action are still under investigation.
  • Understanding solute-protein interactions is crucial for comprehending protein folding, stability, and function.

Purpose of the Study:

  • To quantify the binding affinity of urea to different amino acid residues and peptide backbones.
  • To elucidate the thermodynamic basis of urea-induced protein denaturation.
  • To develop a general equation linking urea binding constants to free energy changes.

Main Methods:

  • Measurement of partial molar volumes and adiabatic compressibilities of amino acid derivatives and oligoglycines in varying urea concentrations.
  • Analysis of experimental data using statistical thermodynamic formalism.

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  • Determination of association constants (k) for urea binding.

    • Main Results:

    • Association constants (k) for urea binding ranged from 0.04 to 0.39 M.
    • Derived a general equation linking binding constants (k) to the change in free energy of transfer (ΔGtr).
    • Found that solute-solute interactions (ΔΔGI) and cavity formation (ΔΔGC) significantly influence the net transfer free energy.

    Conclusions:

    • Data support a direct interaction model where urea denatures proteins through favorable interactions with diverse protein groups.
    • The derived equation highlights the strong influence of solute concentration on interaction free energies.
    • Caution is advised when comparing transfer free energies of solutes with differing solubilities.