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Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
A periodic table of coiled-coil protein structures
Efrosini Moutevelis1, Derek N Woolfson
1School of Chemistry, University of Bristol, Bristol BS8 1TS, UK.
Journal of Molecular Biology
|December 9, 2008
Summary
Researchers created a "periodic table of coiled coils" to classify protein structures. This new classification system organizes coiled-coil assemblies by complexity and helix number, aiding future protein design.
Area of Science:
- Structural biology
- Biochemistry
- Bioinformatics
Background:
- Coiled coils are protein structural motifs essential for various biological functions.
- These structures feature two or more alpha-helices packed via knob-into-hole side chain interactions.
- Understanding coiled coil diversity is crucial for protein engineering.
Purpose of the Study:
- To systematically analyze and classify a comprehensive set of coiled-coil protein structures.
- To develop a user-friendly resource for exploring coiled coil diversity and properties.
- To establish a foundation for future coiled coil prediction and design endeavors.
Main Methods:
- Combined automated and manual analysis of known coiled-coil structures.
- Developed a classification system based on the number of alpha-helices and complexity.
- Created an online database and visualization tool, the "periodic table of coiled coils".
Main Results:
- A systematic classification of coiled-coil protein structures was established.
- The classification organizes assemblies by the number of helices (columns) and complexity (rows).
- An interactive online resource (http://coiledcoils.chm.bris.ac.uk/ccplus/search/periodic_table) was launched.
Conclusions:
- The "periodic table of coiled coils" provides a framework for understanding coiled coil structural possibilities and limitations.
- This resource facilitates future studies in coiled coil prediction, engineering, and de novo design.
- The classification advances the understanding of protein structure-function relationships.
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