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Globular Proteins

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...

Globular and Fibrous Proteins

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

Globular and Fibrous Proteins

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

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...

Protein Folding

Protein Folding

Protein Folding

Protein Folding

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Related Experiment Video

Updated: May 22, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Globularity and protein function.

¹a Chemistry Department , Princeton University , Princeton , NJ , 08544-1009.

Journal of Biomolecular Structure & Dynamics

|May 22, 2012

Summary

This summary is machine-generated.

Protein folding typically results in compact, globular structures with distinct hydrophobic cores. Examining exceptions to this rule offers new insights into protein structure and function relationships.

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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

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4D Imaging of Protein Aggregation in Live Cells

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Published on: April 5, 2013

Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Protein folding is driven by forces that generally produce compact, globular structures.
These native protein structures typically exhibit a hydrophobic interior and a polar exterior.

Purpose of the Study:

To investigate apparent exceptions to the typical globular and compact protein structure.
To explore the relationship between protein structure and function in these exceptional cases.

Main Methods:

Analysis of known protein structures.
Comparative structural analysis of globular and non-globular proteins.
Structure-function relationship studies.

Main Results:

Most proteins fold into predictable globular and compact forms.
Certain proteins deviate from this general rule, presenting unique structural characteristics.
These exceptions provide valuable information for understanding protein function.

Conclusions:

The near-universality of globular protein structures highlights the importance of exceptions.
Studying atypical protein structures enhances our understanding of protein function.
Protein structure-function links are complex and include non-canonical examples.