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Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...

Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...

Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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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.
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Protein Organization

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Related Experiment Video

Updated: Jun 20, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

Structure-function analysis of human protein Ero1-Lalpha.

Yanyan Chu¹, Charles Yang, Xianjun Chen

¹Department of Pharmaceutical Sciences, School of Pharmacy, East China University of Science and Technology, 130 Meilong Road, Shanghai, China.

Biochemical and Biophysical Research Communications

|September 22, 2009

Summary

Human Ero1-Lalpha is crucial for protein folding, but its structure is unknown. Researchers modeled its structure based on yeast Ero1p, revealing insights into its function and tighter FAD binding compared to its yeast counterpart.

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Last Updated: Jun 20, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

Identification of Functional Protein Regions Through Chimeric Protein Construction

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Human Ero1-Lalpha enzyme is essential for disulfide bond formation and protein folding.
Protein misfolding is implicated in diseases like diabetes, arthritis, cancer, and aging.
The lack of a crystal structure for human Ero1-Lalpha impedes understanding its biological function.

Purpose of the Study:

To build a three-dimensional structural model of human Ero1-Lalpha.
To investigate the structure-function relationships of Ero1-Lalpha.
To compare Ero1-Lalpha with its yeast homolog, Ero1p.

Main Methods:

Homology modeling based on the crystal structure of yeast Ero1p.
Computational analysis of structural characteristics.
Experimental validation of computational findings.

Main Results:

A rational three-dimensional structural model of human Ero1-Lalpha was successfully constructed.
Similarities and differences between Ero1-Lalpha and Ero1p were identified.
Both computational and experimental data indicated tighter binding of FAD with Ero1-Lalpha compared to Ero1p.
A probable electron transfer pathway for Ero1-Lalpha was proposed.

Conclusions:

The developed structural model provides the first insight into the structure-function relationships of Ero1-Lalpha.
Ero1-Lalpha exhibits distinct FAD binding characteristics compared to Ero1p.
Further research into the electron transfer pathway can elucidate Ero1-Lalpha's catalytic mechanism.