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Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

Protein Organization

Protein Organization

Protein Organization

Protein Organization

Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

Nucleic Acid Structure

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...

Protein Folding

Protein Folding

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Related Experiment Video

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Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

CC+: a relational database of coiled-coil structures.

Oliver D Testa¹, Efrosini Moutevelis, Derek N Woolfson

¹School of Chemistry, University of Bristol, Bristol BS8 1TS, UK.

Nucleic Acids Research

|October 10, 2008

Summary

The CC+ DATABASE offers a searchable collection of coiled-coil structures, identified using the SOCKET program. This resource aids protein structure prediction and analysis by providing detailed sequence and structural data.

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Area of Science:

Structural Biology
Bioinformatics
Computational Biology

Background:

Coiled coils are prevalent protein structural motifs crucial for various biological functions.
Accurate identification and analysis of coiled-coil structures are essential for understanding protein-protein interactions and functions.
Existing databases may lack comprehensive data or user-friendly interfaces for exploring coiled-coil information.

Purpose of the Study:

To introduce the CC+ DATABASE, a novel, detailed, and searchable repository for coiled-coil assignments.
To provide researchers with an efficient tool for compiling and interrogating subsets of coiled-coil structures.
To facilitate protein structure prediction and analysis through accessible structural and sequence data.

Main Methods:

Coiled coils were identified using the SOCKET program, which employs a 'knobs-into-holes' packing model.
A new method for determining overall sequence identity was developed to minimize statistical bias in datasets.
The database offers two entry points: the 'Periodic Table of Coiled-coil Structures' and the 'Dynamic Interface' for complex queries.

Main Results:

The CC+ DATABASE provides comprehensive coiled-coil assignments with detailed structural and sequence information.
The 'Dynamic Interface' enables sophisticated, multi-level searches for specific coiled-coil subsets.
Retrieved data can be exported in various formats, including PyMOL/RasMol scripts and Position-Specific Scoring Matrices.

Conclusions:

The CC+ DATABASE serves as a valuable resource for researchers studying coiled-coil structures.
Its advanced search capabilities and data output formats enhance the analysis of protein structures and sequences.
This database supports advancements in protein structure prediction and understanding protein interactions.