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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.3K
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...
1.3K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

1.7K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
1.7K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.6K
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...
19.6K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

47.2K
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
47.2K
Carbon Skeletons01:12

Carbon Skeletons

115.4K
Life on Earth is carbon-based, as all macromolecules that make up living organisms contain carbon atoms. All organic compounds have a carbon backbone. Each carbon atom is tetravalent and can bond with four other atoms, making it an extraordinarily flexible component of biological molecules. Because carbon’s valence electrons are stable, it rarely becomes an ion. As the carbon chain increases in length, structural modifications such as ring structures, double bonds, and branching side...
115.4K
The Extracellular Matrix01:42

The Extracellular Matrix

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Overview
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Updated: Feb 9, 2026

&sup1;H NMR of Conformationally Flexible Molecules: Temporal Resolution
00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.3K

高用量スタチンとIDEAL研究

Uffe Ravnskov, Paul J Rosch, Morley C Sutter

    JAMA
    |June 8, 2006
    PubMed
    まとめ

    No abstract available in PubMed .

    さらに関連する動画

    &sup1;H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
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    ¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

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    Factors Affecting Intrinsically Disordered Proteins
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    Factors Affecting Intrinsically Disordered Proteins

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    関連する実験動画

    Last Updated: Feb 9, 2026

    &sup1;H NMR of Conformationally Flexible Molecules: Temporal Resolution
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    ¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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    &sup1;H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
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    ¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

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    Factors Affecting Intrinsically Disordered Proteins
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    Factors Affecting Intrinsically Disordered Proteins

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