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Related Concept Videos

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
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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
Chair Conformation of Cyclohexane02:02

Chair Conformation of Cyclohexane

The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
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Conformational plasticity and structure/function relationships in cytochromes P450.

Thomas C Pochapsky1, Sophia Kazanis, Marina Dang

  • 1Department of Chemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA. pochapsk@brandeis.edu

Antioxidants & Redox Signaling
|May 8, 2010
PubMed
Summary

Cytochrome P450 enzymes catalyze crucial oxidations. This review compares known P450 structures, suggesting criteria for predicting substrate selectivity and reaction types.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Cytochrome P450s are a large enzyme superfamily catalyzing oxidative additions.
  • Over 8000 P450 sequences exist, but 3D structures are known for few.
  • Despite a common fold, active site flexibility allows diverse substrate accommodation.

Purpose of the Study:

  • To compare known cytochrome P450 structures.
  • To suggest structural criteria for predicting substrate selectivity and reaction types.
  • To discuss the role of dynamic processes in P450 catalysis and selectivity.

Main Methods:

  • Comparison of determined P450 enzyme structures.
  • Review of noncrystallographic methods (mass spectrometry, NMR) for structure and dynamics characterization.

Main Results:

  • All determined P450 structures share a common global fold.
  • Active site flexibility and modularity enable broad substrate specificity and selective oxidations.
  • Structural criteria for predicting substrate selectivity and reaction types are proposed.

Conclusions:

  • Understanding P450 structure-function relationships is key to predicting catalytic outcomes.
  • Dynamic conformational changes are critical for catalytic competence and selectivity.
  • Noncrystallographic methods are valuable for characterizing P450s.