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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....

Protein Organization

Protein Organization

Protein Organization

Protein Organization

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Related Experiment Video

Updated: Mar 27, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

α/β coiled coils.

Marcus D Hartmann¹, Claudia T Mendler¹, Jens Bassler¹

¹Department of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.

|January 16, 2016

Summary

This summary is machine-generated.

Minor mutations to protein coiled coils unexpectedly created a novel alpha/beta structure. This new fiber formation demonstrates that significant structural changes are possible within known protein folds.

Keywords:

biophysics fiber heptad repeat none sequence periodicity structural biology supercoil α-helix

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

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Area of Science:

Protein structure and bioinformatics
Biophysics
Structural biology

Background:

Coiled coils represent a well-understood protein fold with extensively characterized backbone structures.
Parametric equations allow for precise description and manipulation of coiled coil architecture.

Purpose of the Study:

To investigate the structural consequences of inserting residues into parallel, trimeric coiled coils.
To explore the potential for novel protein backbone structures through minor sequence modifications.

Main Methods:

Introduction of two or six residues into the heptad repeat of a parallel, trimeric coiled coil.
Analysis of the resulting structural changes, including fiber formation and backbone conformation.

Main Results:

Unexpected formation of a new fiber type from modified coiled coils.
Local formation of short beta-strands due to insertion-induced strain.
A shift in chain path by 120° around the trimer axis, resulting in an alpha/beta coiled coil.
Retention of only one backbone hydrogen bond per repeat unit.

Conclusions:

Minor mutations can lead to substantially novel backbone structures within allowed Ramachandran space.
The study reveals unexpected structural plasticity in seemingly well-understood protein folds.
Demonstrates the possibility of creating new protein architectures like alpha/beta coiled coils through targeted modifications.