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Related Concept Videos

Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

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 Organization01:13

Protein Organization

Overview
Protein Organization01:24

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 and Protein Structure02:15

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...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

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Analyzing and Building Nucleic Acid Structures with 3DNA
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Published on: April 26, 2013

Sequence repeats and protein structure.

Trinh X Hoang1, Antonio Trovato, Flavio Seno

  • 1Institute of Physics, Vietnam Academy of Science and Technology, 10 Dao Tan, Hanoi 10000, Vietnam.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|December 11, 2012
PubMed
Summary
This summary is machine-generated.

Repeated protein sequences can be intrinsically disordered. Imperfect repeats improve folding for some proteins, explaining nature's use of repeats for versatile, unstructured protein design.

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A Protocol for Computer-Based Protein Structure and Function Prediction
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Published on: November 3, 2011

Area of Science:

  • Computational protein design
  • Protein structure and folding
  • Bioinformatics and sequence analysis

Background:

  • Tandem repeats are common in protein sequences.
  • Sequence conservation in repeats correlates with intrinsic disorder.
  • Understanding sequence-structure relationships in repeats is crucial for protein function.

Purpose of the Study:

  • To investigate the sequence-structure relationship in repeated protein sequences.
  • To analyze the folding properties of proteins with varying repeat imperfections.
  • To explore the role of repeats in designing intrinsically unstructured proteins.

Main Methods:

  • Utilized a coarse-grained protein model with a two-letter amino acid alphabet (hydrophobic/polar).
  • Examined sequence conservation and folding temperatures in simulated repeated sequences.
  • Compared folding properties of perfect versus imperfect repeat sequences.

Main Results:

  • Identified a class of 'bad folders' with significantly lower folding temperatures.
  • Demonstrated that sequence imperfections improve folding for 'bad folders'.
  • Showed that imperfections deteriorate folding properties for 'good folders'.

Conclusions:

  • Sequence imperfections in repeats play a critical role in protein folding.
  • Nature likely utilizes repeat imperfections to design versatile, intrinsically unstructured proteins.
  • Findings provide insights into the evolution and design principles of protein sequences.