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Protein Dynamics in Living Cells

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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Updated: Jan 10, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Dynamic Balance between Protein Core and Solvent Shell: Ultrafast Hemin Dynamics Maps Energy Flow in Non-heme

Shubhangi Majumdar¹, Aastha Razshree¹, Arti Sharma¹

¹Department of Chemistry, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India.

The Journal of Physical Chemistry. B

|November 24, 2025

Summary

Energy flow in proteins like human serum albumin (HSA) and bovine serum albumin (BSA) was studied using hemin chloride. Environmental factors significantly influence energy dissipation dynamics in these biomolecules.

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Area of Science:

Biophysics
Protein Dynamics
Energy Transfer

Background:

Energy flow is crucial for biomolecular processes like catalysis and transport.
Ultrafast energy flow in non-heme proteins is less explored experimentally compared to heme proteins.
Human serum albumin (HSA), bovine serum albumin (BSA), and β-lactoglobulin (β-LG) are important non-heme proteins involved in transport.

Purpose of the Study:

To investigate ultrafast energy flow in HSA, BSA, and β-LG.
To understand the influence of the protein environment on energy dissipation.
To explore the role of solvent and micellar environments on hemin chloride dynamics.

Main Methods:

Incorporation of hemin chloride as a photoreceptor in proteins.
Femtosecond transient absorption spectroscopy to monitor energy dynamics.
Investigation of hemin dynamics in various solvents and micellar systems.

Main Results:

HSA and BSA exhibited different hemin relaxation behaviors due to variations in their binding pockets.
In β-LG, hemin binding at the monomer-monomer interface led to slower energy transfer.
Hydrophobic solvents accelerated energy relaxation, while water slowed it down.
Surfactants and reverse micelles modulated energy dissipation, mimicking biological conditions.

Conclusions:

Subtle environmental changes dramatically alter energy dynamics in proteins.
Understanding these dynamics is fundamental to comprehending biological processes.
Protein-environment interactions play a critical role in regulating energy flow.