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Related Concept Videos

Protein Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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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...
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Dehydration Synthesis01:15

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Intrinsically Disordered Proteins02:18

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Dynamical Transition in Dehydrated Proteins.

Johanna Kölbel1, Moritz L Anuschek1,2, Ivonne Stelzl2

  • 1Department of Chemical Engineering, University of Cambridge, Cambridge CB3 0AS, U.K.

The Journal of Physical Chemistry Letters
|March 25, 2024
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Summary
This summary is machine-generated.

Dry biomolecules exhibit temperature-dependent dynamics, showing anharmonic motions linked to unfolding and jamming. Experiments found no evidence of Fröhlich coherence in these systems.

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Area of Science:

  • Biophysics
  • Materials Science
  • Spectroscopy

Background:

  • Understanding biomolecular dynamics is crucial for biological function.
  • Solvent effects often mask intrinsic molecular dynamics.
  • Terahertz spectroscopy offers a unique window into molecular motions.

Purpose of the Study:

  • To investigate the dynamics of dry biomolecules, decoupled from solvent effects.
  • To identify temperature-dependent changes in molecular motion.
  • To explore the potential role of anharmonicity and Fröhlich coherence in dry biomolecules.

Main Methods:

  • Terahertz time-domain spectroscopy (THz-TDS) to probe molecular vibrations.
  • Differential scanning calorimetry (DSC) to measure thermal properties.
  • Analysis of spectral signatures below and above the boson peak.

Main Results:

  • Lyophilized sucrose showed increased absorption with temperature, indicating anharmonic excitations.
  • Polypeptides and proteins (bacitracin, lysozyme, human serum albumin) displayed complex temperature dependencies.
  • Evidence of anharmonic motions, associated with partial unfolding and molecular jamming, was observed in dry biomolecules.
  • Protein modes activated at temperatures near the dynamical transition, even without hydration.
  • No evidence for Fröhlich coherence was detected.

Conclusions:

  • Anharmonic motions play a significant role in the temperature-dependent behavior of dry biomolecules.
  • Partial unfolding and molecular jamming occur in dry proteins at elevated temperatures.
  • The absence of hydration does not preclude the activation of protein molecular modes.
  • The study did not find support for the Fröhlich coherence mechanism in the investigated dry biomolecules.