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Related Concept Videos

Globular Proteins01:27

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 Proteins02:21

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 Proteins02:21

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 Folding01:22

Protein Folding

Overview
Protein Folding01:25

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 Folding01:22

Protein Folding

Overview

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Structures closed into cycles in globular proteins.

A V Efimov1

  • 1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia. efimov@protres.ru

Biochemistry. Biokhimiia
|February 21, 2012
PubMed
Summary
This summary is machine-generated.

Protein structures frequently form closed cycles and cylinders, enhancing stability and cooperative function. This cyclic organization, seen in motifs like beta-hairpins and tertiary structures, explains their prevalence in proteins.

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Area of Science:

  • Structural biology
  • Protein folding
  • Biophysics

Background:

  • Proteins exhibit diverse cyclic structures at multiple organizational levels.
  • Simple motifs like beta-hairpins and βαβ-units form cycles via hydrogen bonds.
  • Complex motifs arise from secondary cyclization of simpler units.

Purpose of the Study:

  • To investigate the prevalence and functional significance of cyclic structures in proteins.
  • To understand how cyclization contributes to protein stability and cooperativity.
  • To identify common cyclic motifs across different levels of protein organization.

Main Methods:

  • Analysis of protein structural databases.
  • Identification and classification of cyclic structural motifs.
  • Comparison of stability and functional properties between cyclic and open structures.

Main Results:

  • Cyclic structures are widespread at secondary and tertiary levels of protein organization.
  • Simple cyclic motifs include beta-hairpins, triple-stranded beta-sheets, and βαβ-units.
  • Complex cyclic motifs like abcd-units and φ-motifs are formed through secondary cyclization.
  • Proteins and domains often fold into cylinder-like cyclic structures.
  • Cyclic organization enhances structural stability and cooperativity compared to open structures.

Conclusions:

  • The prevalence of cyclic motifs in proteins is attributed to their increased stability and cooperativity.
  • Cyclization is a fundamental principle in protein architecture, contributing to functional efficiency.
  • Understanding cyclic protein structures provides insights into protein evolution and design.