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Cryo-electron Microscopy01:28

Cryo-electron Microscopy

Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...

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A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering
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Published on: December 7, 2016

Measuring and modeling hemoglobin aggregation below the freezing temperature.

Mónica Rosa1, Carlos Lopes, Eduardo P Melo

  • 1Centro de Química Estrutural, Department of Chemical Engineering, Instituto Superior Técnico, Lisboa 1049-001, Portugal.

The Journal of Physical Chemistry. B
|July 2, 2013
PubMed
Summary
This summary is machine-generated.

Studying protein stability below freezing is challenging. An isochoric method allows observation of protein aggregation at sub-freezing temperatures, revealing aggregation mechanisms and aiding formulation development.

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Protein Science

Background:

  • Protein solutions require freezing for storage and transport, but freezing poses risks to protein integrity.
  • Studying protein stability below freezing is difficult due to phase separation limiting solute concentration.

Purpose of the Study:

  • To develop an isochoric method for studying protein aggregation in solutions below the freezing point.
  • To investigate the thermodynamics and mechanism of protein aggregation at sub-freezing temperatures.

Main Methods:

  • Developed an isochoric method to maintain aqueous solutions unfrozen below 0°C by increasing pressure in a fixed volume.
  • Studied aggregation rates of bovine hemoglobin (BHb) at various temperatures (-5 to -20°C) and concentrations.
  • Utilized fluorescence spectroscopy to determine BHb unfolding thermodynamics.
  • Applied a mathematical model to describe and predict BHb aggregation kinetics.

Main Results:

  • Isochoric method enabled protein aggregation studies below freezing.
  • BHb aggregation rates increased at lower temperatures and higher concentrations.
  • Sucrose addition significantly reduced BHb aggregation, preventing it at 300 g/L.
  • Aggregation is mediated by an unfolded state, followed by rapid aggregate growth and precipitation.

Conclusions:

  • The isochoric method provides fundamental thermodynamic and mechanistic insights into protein aggregation below freezing.
  • This approach offers a new strategy for accelerated formulation studies of proteins at sub-freezing temperatures.
  • Understanding cold denaturation and aggregation is crucial for optimizing protein stability during storage and transport.