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Related Experiment Video

Updated: Jun 10, 2026

Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications

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Reversible dioxygen binding in solvent-free liquid myoglobin.

Adam W Perriman¹, Alex P S Brogan, Helmut Cölfen

¹Centre for Organized Matter Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, UK.

Nature Chemistry

|July 24, 2010

Summary

Researchers created room-temperature, solvent-free myoglobin liquids. These liquids maintain near-native structure and reversible dioxygen binding, offering new possibilities for protein-based nanotechnology.

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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

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Published on: April 14, 2015

Area of Science:

Biochemistry
Structural Biology
Materials Science

Background:

Protein structure and function are intrinsically linked to aqueous environments.
Denaturation and loss of function occur under non-native conditions like dehydration or heat.
Functional metalloproteins in solvent-free liquids are previously unknown.

Purpose of the Study:

To synthesize and characterize room-temperature, solvent-free myoglobin liquids.
To assess the structural integrity and functional activity of myoglobin in a solvent-free state.
To explore potential applications in nanoscience and bionanotechnology.

Main Methods:

Synthesis of room-temperature, solvent-free myoglobin liquids.
Structural analysis to confirm near-native protein conformation.
Functional assays to evaluate dioxygen binding capacity.

Main Results:

Successfully created stable, room-temperature solvent-free myoglobin liquids.
Myoglobin retained near-native structure in the solvent-free liquid state.
Dioxygen binding ability was equivalent to physiological conditions and reversible.

Conclusions:

Demonstrated the feasibility of functional metalloproteins in solvent-free liquids.
Challenges existing theories on the role of solvent in protein structure and function.
Opens new avenues for protein-based nanoscience and bionanotechnology.