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Updated: Jun 28, 2026

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing
Published on: July 3, 2016
SPROUTS: a database for the evaluation of protein stability upon point mutation
Mathieu Lonquety1, Zoé Lacroix, Nikolaos Papandreou
1Scientific Data Management Laboratory, Arizona State University, Tempe AZ 85282-5706, USA.
SPROUTS is a new database offering integrated protein structural analyses, including Most Interacting Residues (MIR) and Tightened End Fragments (TEF). It aids in understanding protein folding and mutation effects.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Protein structure and folding are fundamental to biological function.
- Predicting protein folding pathways and the impact of mutations is a significant challenge.
- Existing databases lack integrated analyses of protein structural data.
Purpose of the Study:
- To introduce SPROUTS, a novel database for comprehensive protein structural analysis.
- To provide integrated access to diverse structural data and prediction tools.
- To facilitate the study of protein folding nuclei and mutation effects.
Main Methods:
- SPROUTS integrates data for 429 representative protein structures.
- It includes predictions of Most Interacting Residues (MIR) for folding nuclei.
- The database incorporates Tightened End Fragments (TEF) and free energy change calculations upon mutation.
Main Results:
- SPROUTS offers a centralized platform for multiple structural analyses.
- Users can access, visualize, and download data in various formats (text, Excel, 3D structures).
- The database enables detailed analysis of protein folding characteristics and mutation impacts.
Conclusions:
- SPROUTS is a unique resource for exploring protein folding mechanisms.
- It provides state-of-the-art tools for analyzing protein structure and mutation effects.
- The database enhances accessibility to advanced protein structural bioinformatics.
Related Concept Videos
In vitro Mutagenesis
In-vitro Mutagenesis
Spontaneous and Induced Mutations
Point and Frameshift Mutations
Mutations in Microorganisms
Protein Denaturation
