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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
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...
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 Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

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Published on: July 25, 2013

CyloFold: secondary structure prediction including pseudoknots.

Eckart Bindewald1, Tanner Kluth, Bruce A Shapiro

  • 1Basic Science Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, MD 21702, USA.

Nucleic Acids Research
|May 27, 2010
PubMed
Summary

This study introduces a novel computational method for RNA secondary structure prediction that handles complex pseudoknots. The approach simulates RNA folding and checks for steric feasibility, offering a competitive alternative to existing tools.

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Area of Science:

  • Computational biology
  • Molecular modeling
  • Bioinformatics

Background:

  • RNA secondary structure prediction is crucial for understanding RNA function.
  • Existing methods often limit pseudoknot complexity due to computational constraints.
  • Handling complex pseudoknots remains a significant challenge in the field.

Purpose of the Study:

  • To develop a computational method for RNA secondary structure prediction without restrictions on pseudoknot complexity.
  • To incorporate a steric feasibility check within the folding simulation.
  • To evaluate the performance of the new method against established RNA structure prediction tools.

Main Methods:

  • Simulating RNA folding in a coarse-grained manner.
  • Selecting helices based on established energy rules.
  • Utilizing a coarse-grained 3D model to assess steric feasibility during folding.

Main Results:

  • The developed method demonstrates competitive performance on datasets of 26 and 241 RNA sequences.
  • It successfully predicts RNA secondary structures with complex pseudoknots.
  • The approach shows comparable accuracy to pknotsRG, HotKnots, and UnaFold.

Conclusions:

  • The new method overcomes algorithmic limitations in pseudoknot prediction.
  • It provides a robust tool for RNA secondary structure prediction with complex pseudoknots.
  • The integration of steric feasibility testing enhances prediction accuracy and reliability.