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RNA Stability

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Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...

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Related Experiment Video

Updated: Feb 27, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Exploiting sequence and stability information for directing nanobody stability engineering.

Patrick Kunz¹, Tilman Flock², Nicolas Soler³

¹Division of Functional Genome Analysis, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 580, 69120 Heidelberg, Germany.

Biochimica Et Biophysica Acta. General Subjects

|June 24, 2017

Summary

This summary is machine-generated.

Engineering nanobody thermostability through sequence analysis can enhance protein stability by up to 6.1°C. This study reveals a mutational strategy for improving nanobody biophysical behavior and highlights species-specific architectural differences.

Keywords:

Protein aggregation Protein design Protein engineering Protein stability Single-domain antibody (sdAb, nanobody)

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Area of Science:

Biotechnology
Protein Engineering
Structural Biology

Background:

Camelid heavy-chain antibodies, known as nanobodies, possess significant biotechnological potential.
Improving nanobody thermostability is crucial for applications in research, diagnostics, and therapy, impacting conformational stability, protease resistance, and aggregation.

Purpose of the Study:

To identify and experimentally validate amino acid variations that enhance nanobody thermostability.
To understand the mechanisms underlying nanobody stabilization and investigate discrepancies between predicted and experimental outcomes.

Main Methods:

Analysis of sequences and thermostabilities of 78 purified nanobody binders.
Experimental validation of potentially stabilizing amino acid variations.

Main Results:

Identified mutations improving nanobody stability by an average of 2.3°C, with a maximum increase of 6.1°C.
Stabilization mechanisms involve enhanced conformational stability and improved aggregation behavior.
Observed instances where predicted stabilizing mutations led to thermal destabilization, prompting further investigation.

Conclusions:

Developed a mutational strategy to enhance the biophysical properties of nanobody binders.
Demonstrated species-specificity in nanobody architecture.
Highlighted the potential and limitations of engineering nanobody thermostability using sequence and stability data.