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Related Concept Videos

Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)01:22

Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)

Vicinal or three-bond coupling is commonly observed between protons attached to adjacent carbons. Here, nuclear spin information is primarily transferred via electron spin interactions between adjacent C‑H bond orbitals. This generally favors the antiparallel arrangement of spins, so 3J values are usually positive.
The extent of coupling depends on the C‑C bond length, the two H‑C‑C angles, any electron-withdrawing substituents, and the dihedral angle between the involved orbitals. The...
Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)01:20

Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)

Two NMR-active nuclei bonded to a central atom can be involved in geminal or two-bond coupling. Geminal coupling is commonly seen between diastereotopic protons in chiral molecules and unsymmetrical alkenes, among others.
The central atom need not be NMR-active because its electrons are affected by the electron polarization of the spin-active atoms. However, spin information is transmitted less effectively than in one-bond coupling, and 2J values are usually weaker than 1J values. The energy of...
Spin–Spin Coupling: One-Bond Coupling01:17

Spin–Spin Coupling: One-Bond Coupling

Coupling interactions are strongest between NMR-active nuclei bonded to each other, where spin information can be transmitted directly through the pair of bonding electrons. While nuclei polarize their electrons to the opposite spins, the bonding electron pair has opposite spins. Configurations with antiparallel nuclear spins are expected to be lower in energy. When coupling makes antiparallel states more favorable, J is considered to have a positive value. The one-bond coupling constant, 1J,...
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

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

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...

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Related Experiment Video

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The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)
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Evolutionary coupling in the K(V)1.2-β₂ complex.

Shreedhar Natarajan1, Robert J Mashl, Eric Jakobsson

  • 1University of Illinois at Urbana-Champaign, USA.

Channels (Austin, Tex.)
|September 7, 2010
PubMed
Summary
This summary is machine-generated.

We identified key interactions in the K(V)1.2/β₂ potassium channel complex, revealing how cell redox state links to membrane electrical activity and hypoxia response.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Ion Channel Science

Background:

  • The K(V)1.2 potassium channel's oxygen sensing is modulated by beta subunits, homologous to oxidoreductases.
  • The mechanism linking cellular redox state to membrane electrical activity via K(V)1.2/β₂ coupling remains unclear.

Purpose of the Study:

  • To elucidate the interaction network regulating the K(V)1.2/β₂ complex's response to hypoxia.
  • To identify specific motifs involved in channel function and hypoxia response.

Main Methods:

  • Applied evolutionary correlation analysis to infer protein interactions.
  • Analyzed correlated amino acid substitutions in orthologous proteins across species.
  • Utilized significance testing to validate correlation findings.

Main Results:

  • Characterized a statistically significant network of motif interactions between K(V)1.2 (α) and β₂ subunits.
  • Identified correlations between K(V)1.2/β₂ motifs and those in RACK1 and Eif36sip, linking to hypoxia response.
  • Established biological relevance of observed correlations.

Conclusions:

  • The study reveals novel insights into multi-protein complex function and ion channel-mediated cellular communication.
  • Identified specific motifs as potential experimental targets for studying hypoxia response in ion channels.
  • Demonstrated the utility of evolutionary correlation analysis for inferring protein domain-domain interactions.