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Related Experiment Video

Updated: Feb 10, 2026

Optimization of Crystal Growth for Neutron Macromolecular Crystallography

Optimization of Crystal Growth for Neutron Macromolecular Crystallography

Published on: March 13, 2021

Macromolecular mimicry.

P Nissen¹, M Kjeldgaard, J Nyborg

¹Institute of Molecular and Structural Biology, University of Aarhus, Gustav Wieds vej 10C, DK-8000 Aarhus C, Denmark.

The EMBO Journal

|February 17, 2000

Summary

This summary is machine-generated.

Proteins can mimic nucleic acid structures, even impacting ribosome function during protein synthesis. This molecular mimicry may be widespread, offering insights into protein biosynthesis evolution.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Proteins are known to exhibit structural similarities to nucleic acids.
This phenomenon, termed macromolecular mimicry, has been observed in various biological contexts.
Specific examples exist within the protein biosynthesis machinery, such as on the ribosome.

Purpose of the Study:

To explore the generality of macromolecular mimicry between proteins and nucleic acids.
To investigate if this mimicry extends beyond protein biosynthesis.
To discuss the functional and evolutionary implications of this mimicry.

Main Methods:

Comparative structural analysis of proteins and nucleic acids.
Review of existing structural data and experimental findings.
Functional and evolutionary analysis of observed mimicry.

Main Results:

Evidence suggests that some proteins structurally mimic nucleic acids.
Macromolecular mimicry is observed in proteins interacting with the ribosome.
Emerging structural data indicates mimicry may occur outside protein biosynthesis.

Conclusions:

Macromolecular mimicry between proteins and nucleic acids is a potentially general phenomenon.
This mimicry has significant implications for understanding the evolution of protein biosynthesis.
Further structural studies are needed to fully elucidate the scope and impact of mimicry.