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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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...
Protein Folding01:25

Protein Folding

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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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A surprising role for conformational entropy in protein function.

A Joshua Wand1, Veronica R Moorman, Kyle W Harpole

  • 1Graduate Group in Biochemistry & Molecular Biophysics, The Johnson Research Foundation and Department of Biochemistry & Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA, 19104-6059, USA, wand@mail.med.upenn.edu.

Topics in Current Chemistry
|March 13, 2013
PubMed
Summary

Understanding protein-ligand interactions is key for enzymatic reactions. New nuclear magnetic resonance (NMR) methods measure protein motion to reveal conformational entropy, offering insights into protein function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • High-affinity protein-ligand complex formation is essential for enzymatic reactions.
  • Calculating the energetics of protein-ligand interactions solely from molecular structure is challenging.
  • Protein conformational entropy is a difficult-to-measure yet crucial component of binding free energy.

Purpose of the Study:

  • To review experimental approaches for characterizing fast internal protein motion.
  • To explain how protein motion data can provide insights into conformational entropy.
  • To discuss current findings and future directions in using motion as a proxy for entropy.

Main Methods:

  • Solution nuclear magnetic resonance (NMR) relaxation techniques.
  • Measuring protein internal dynamics and conformational exchange.
  • Utilizing motion data as a proxy for conformational entropy.

Main Results:

  • Recent advances in NMR relaxation enable quantification of protein motion.
  • Protein motion measures serve as a proxy for conformational entropy.
  • This approach offers new perspectives on protein-ligand interactions and function.

Conclusions:

  • Characterizing protein motion via NMR relaxation is a powerful tool.
  • This method provides valuable insights into conformational entropy.
  • Emerging views of protein function are being shaped by understanding internal dynamics.