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Related Concept Videos

Acid-Base Titration Curves02:23

Acid-Base Titration Curves

141.2K
A titration curve is a plot of some solution property versus the amount of added titrant. For acid-base titrations, solution pH is a useful property to monitor because it varies predictably with the solution composition and, therefore, may be used to monitor the titration’s progress and detect its endpoint. Acid-base titration can be performed with a strong acid and a strong base, a strong acid and a weak base, or a strong base and a weak acid.
For a titration carried out for 25.00 mL of...
141.2K
Titration Calculations: Weak Acid - Strong Base03:55

Titration Calculations: Weak Acid - Strong Base

49.3K
Calculating pH for Titration Solutions: Weak Acid/Strong Base
For the titration of 25.00 mL of 0.100 M CH3CO2H with 0.100 M NaOH, the reaction can be represented as:
49.3K
Redox Titration: Other Oxidizing and Reducing Agents01:26

Redox Titration: Other Oxidizing and Reducing Agents

1.4K
Besides iodine, other oxidizing or reducing agents can serve as titrants in redox titrations. Common oxidizing titrants include KMnO4, cerium(IV), and K2Cr2O7. The choice of oxidizing titrants depends on factors like stability, cost, analyte strength, and reaction rate between the analyte and titrant. KMnO4 is a strong oxidizing titrant that reduces from Mn(VII) to Mn(II) in a highly acidic solution, simultaneously oxidizing the analyte to a higher oxidation state. In this case, KMnO4 acts as a...
1.4K
Conformity01:20

Conformity

48.2K
Conformity is the change in a person’s behavior to go along with the group, even if that person does not agree with the group.
48.2K
Titration Calculations: Strong Acid - Strong Base02:28

Titration Calculations: Strong Acid - Strong Base

33.9K
Calculating pH for Titration Solutions: Strong Acid/Strong Base
A titration is carried out for 25.00 mL of 0.100 M HCl (strong acid) with 0.100 M of a strong base NaOH. The pH at different volumes of added base solution can be calculated as follows:
(a) Titrant volume = 0 mL. The solution pH is due to the acid ionization of HCl. Because this is a strong acid, the ionization is complete and the hydronium ion molarity is 0.100 M. The pH of the solution is then:
33.9K
Titration of a Polyprotic Acid02:08

Titration of a Polyprotic Acid

105.2K
A polyprotic acid contains more than one ionizable hydrogen and undergoes a stepwise ionization process.  If the acid dissociation constants of the ionizable protons differ sufficiently from each other, then the titration curve for such polyprotic acid generates a distinct equivalence point for each of its ionizable hydrogens. Therefore, titration of a diprotic acid results in the formation of two equivalence points, whereas the titration of a triprotic acid results in the formation of three...
105.2K

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Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding
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Tracking Conformational Changes in Phosvitin throughout a Crowding-Agent-Based Titration.

Evelien Van de Vondel1, Wouter Herrebout1, Christian Johannessen1

  • 1Molecular Spectroscopy Group, Department of Chemistry, University of Antwerp, Groenenborgerlaan 171, 2020, Antwerp, Belgium.

Chembiochem : a European Journal of Chemical Biology
|November 20, 2018
PubMed
Summary

Raman optical activity (ROA) effectively tracks subtle protein structure changes. Different crowding agents like Ficoll-70 and dextran-70 impact phosvitin structure differently, with Ficoll-70 showing more pronounced effects.

Keywords:
Raman optical activityconformation analysisdisorderprotein structuresstructural biology

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Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Intrinsically disordered proteins (IDPs) play crucial roles in cellular processes.
  • Understanding conformational dynamics of IDPs is vital for elucidating their function.
  • Crowding agents are used to mimic cellular environments and study protein behavior.

Purpose of the Study:

  • To investigate the sensitivity of Raman optical activity (ROA) in detecting small conformational changes in proteins.
  • To explore the structural alterations in the intrinsically disordered protein phosvitin under varying concentrations of crowding agents.
  • To compare the effects of different crowding agents, Ficoll-70 and dextran-70, on phosvitin's structure.

Main Methods:

  • Utilized Raman optical activity (ROA) spectroscopy to monitor protein structure.
  • Employed phosvitin, an intrinsically disordered protein, as the model system.
  • Introduced varying concentrations of Ficoll-70 and dextran-70 as crowding agents.

Main Results:

  • ROA successfully detected subtle conformational changes in phosvitin, including alterations in beta-sheet and alpha-helical structures.
  • Significant differences were observed in the structural responses of phosvitin to Ficoll-70 and dextran-70.
  • Ficoll-70 induced more pronounced structural changes in phosvitin, observable at lower concentrations.
  • Some spectral variations were attributed to interactions between phosphorylated residues and the crowding agent, rather than secondary structure changes.

Conclusions:

  • ROA is a sensitive technique for tracking small conformational shifts in proteins.
  • Crowding agents exhibit distinct effects on protein structure, influencing secondary structural elements.
  • The interactions between proteins and crowding agents can lead to spectral changes not solely related to secondary structure modifications.