Related Experiment Video

Updated: Aug 13, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Do vibrational spectroscopies uniquely describe protein dynamics? The case for myoglobin

W Bialek, R F Goldstein

    Biophysical Journal
    |December 1, 1985
    PubMed

    More Related Videos

    NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins09:25

    NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

    Published on: November 1, 2024

    Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules10:23

    Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

    Published on: April 25, 2025

    Related Concept Videos

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

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

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

    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.
    IR Spectroscopy: Molecular Vibration Overview01:24

    IR Spectroscopy: Molecular Vibration Overview

    When Infrared (IR) radiation passes through a covalently bonded molecule, the bonds transition from lower to higher vibrational levels. The fundamental vibrational motions that result in infrared absorption can be classified as stretching or bending vibrations.
    Stretching vibrations are vibrational motions that occur along the bond line, changing the bond length or distance between two bonded atoms. They are further distinguished as symmetric or asymmetric. In symmetric stretching, the...
    IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

    IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

    A covalently bonded heteronuclear diatomic molecule can be modeled as two vibrating masses connected by a spring. The vibrational frequency of the bond can be expressed using an equation derived from Hooke's law, which describes how the force applied to stretch or compress a spring is proportional to the displacement of the spring. In this case, the atoms behave like masses, and the bond acts like a spring.
    According to Hooke's law, the vibrational frequency is directly proportional to the...
    Protein Dynamics in Living Cells01:19

    Protein Dynamics in Living Cells

    Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
    Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
    Globular Proteins01:27

    Globular Proteins

    In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
    Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...