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Updated: Jul 8, 2026

A Modified Yeast-one Hybrid System for Heteromeric Protein Complex-DNA Interaction Studies
10:47

A Modified Yeast-one Hybrid System for Heteromeric Protein Complex-DNA Interaction Studies

Published on: July 24, 2017

協同宿主/ゲストの相互作用は,カウンテリオン・アシスタント・ケレーションによる:超分子暗号のシドオロタキサン

Jason W Jones1, Lev N Zakharov, Arnold L Rheingold

  • 1Department of Chemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0212, USA.

Journal of the American Chemical Society
|November 7, 2002
PubMed
まとめ

クラウンエーテルとパラクワット複合体に特定のアニオンを加えると,それらの相互作用が著しく強化されます. この超分子化学的アプローチは,協力的なケラ化によって宿主-ゲスト複合体を安定させ,結合親和性を高めます.

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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

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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¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons

Protons in identical electronic environments within a molecule are chemically equivalent and have the same chemical shift. The replacement test is a useful tool to identify chemical equivalence and predict NMR spectra. A substituent replaces each of the protons being examined and the resulting molecules are compared. If the same molecule is obtained, the protons are equivalent or homotopic. Replacement of any hydrogens in ethane by chlorine yields chloroethane because all six protons are...
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Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

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Spin–Spin Coupling Constant: Overview

In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
Qualitatively, any spin plus-half nucleus polarizes the spins of its electrons to the minus-half state. Consequently, the paired electron in the hydrogen–carbon bond must have a...