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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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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...

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Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

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Sizing up single-molecule enzymatic conformational dynamics.

¹Bowling Green State University, Center for Photochemical Sciences, Department of Chemistry, Bowling Green, OH 43403, USA. hplu@bgsu.edu.

Chemical Society Reviews

|December 6, 2013

Summary

This summary is machine-generated.

Single-molecule enzymology reveals complex protein dynamics in real-time. New techniques allow active manipulation of enzyme reactions and conformational changes for deeper biological insights.

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Area of Science:

Biochemistry
Biophysics
Molecular Biology

Background:

Enzymatic reactions and protein conformational dynamics are crucial for biological functions but challenging to study using traditional ensemble-averaged methods.
Complex enzymatic processes involving multiple steps and conformations are difficult to characterize with conventional techniques.
Understanding the interplay between protein dynamics and enzymatic activity is a central challenge in modern enzymology.

Purpose of the Study:

To highlight the advancements in single-molecule approaches for dissecting complex enzymatic and protein conformational dynamics.
To showcase the evolution of single-molecule enzymology over the past two decades.
To introduce the potential of actively manipulating enzymatic dynamics at the single-molecule level.

Main Methods:

Real-time single-molecule spectroscopy and imaging techniques.
Development of advanced single-molecule methodologies and theoretical analyses.
Biological preparation and characterization of enzyme protein systems.

Main Results:

Single-molecule approaches enable the dissection of complex enzymatic reaction dynamics and protein conformational changes in real-time.
Enzymatic reactions can now be studied at the single-molecule level under physiological conditions.
Active manipulation of enzymatic conformational changes and energy landscapes can regulate enzymatic reactivity.

Conclusions:

Single-molecule enzymology provides powerful tools to overcome limitations of ensemble-averaged studies.
Technological and methodological advancements have propelled the field of protein dynamics research.
Active manipulation and observation of enzymatic dynamics at the single-molecule level open new avenues for understanding complex biological processes.