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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.
A protein's shape is critical to its function. For example, an enzyme can...

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 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.

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Updated: Jun 20, 2026

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

Structural patterns in alpha helices and beta sheets in globular proteins.

Nicholus Bhattacharjee¹, Parbati Biswas

¹Department of Chemistry, University of Delhi, Delhi-110007, India.

Protein and Peptide Letters

|August 20, 2009

Summary

Protein structure analysis reveals alpha-helices and beta-sheets have complementary distributions. Their amino acid properties correlate with these patterns, impacting protein design.

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Published on: November 21, 2013

Area of Science:

Biochemistry and Structural Biology
Computational Biology

Background:

Proteins are fundamental biological molecules composed primarily of secondary structural elements such as alpha-helices and beta-sheets.
Understanding the distribution and characteristics of these elements is crucial for comprehending protein structure-function relationships.

Purpose of the Study:

To conduct a systematic, position-wise analysis of the structural and sequence features of alpha-helices and beta-sheets within proteins.
To investigate the relationship between amino acid properties and the occurrence of these secondary structures.

Main Methods:

Analysis of protein sequence and structural data to identify alpha-helices and beta-sheets.
Calculation of conformational parameters for amino acids within these secondary structures.
Correlation analysis of secondary structure distribution with properties like hydrophobicity, temperature-factor, and relative entropy.

Main Results:

Alpha-helices and beta-sheets exhibit a complementary distribution pattern along the protein chain.
Specific amino acid conformational parameters are associated with their presence in helices or sheets.
Hydrophobicity, temperature-factor, and relative entropy show correlations with secondary structure distribution.

Conclusions:

The distribution of secondary structures in proteins is influenced by intrinsic amino acid properties.
These findings provide insights into the conservation and variation of protein secondary structures.
The study has potential implications for the field of de novo protein design.