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Related Experiment Video

Updated: Aug 1, 2025

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Exploiting conformational dynamics to modulate the function of designed proteins.

Enrico Rennella^1,2,3, Danny D Sahtoe^4,5,6, David Baker^4,5,6

¹Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.

Proceedings of the National Academy of Sciences of the United States of America

|April 24, 2023

Summary

This summary is machine-generated.

Understanding protein dynamics is key for designing proteins with specific functions. This study shows how protein motion affects function and how to control it for new molecular designs.

Keywords:

NMR spectroscopy chemical exchange saturation transfer conformational dynamics ligand binding protein design

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

Biochemistry
Structural Biology
Protein Design

Background:

Artificial intelligence has advanced protein structure prediction from amino acid sequences.
Protein dynamics, encoded in the primary sequence, are crucial for predicting and designing protein function.
Understanding dynamics informs protein design beyond static structures, including excited states influencing function.

Purpose of the Study:

To investigate the role of protein dynamics in modulating the function of the designed protein C34.
To determine the structures of predominant conformations sampled by C34 and their effect on ligand binding affinity.
To engineer an allosterically regulated peptide binder by exploiting observed protein motion.

Main Methods:

Utilized nuclear magnetic resonance (NMR) spectroscopy to observe regions of C34 in conformational exchange.
Employed a mutagenesis approach to stabilize C34 into a single conformation for structural determination.
Developed an allosteric regulator by leveraging the dynamic properties of C34.

Main Results:

Identified predominant conformations of C34, revealing that these conformations attenuate affinity for cognate peptides.
Demonstrated that protein dynamics significantly influence C34's functional properties.
Successfully engineered an allosterically regulated peptide binder with tunable binding affinity.

Conclusions:

Protein dynamics play a critical role in modulating protein function and ligand binding.
NMR spectroscopy is invaluable for guiding protein design and creating molecules with complex functionalities.
Exploiting protein dynamics enables the development of novel, controllable molecular binders.