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Related Concept Videos

Protein Folding01:25

Protein Folding

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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...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA...
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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...
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Protein Organization01:24

Protein Organization

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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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Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Updated: Jul 26, 2025

Microfluidic Mixers for Studying Protein Folding
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Microfluidic Mixers for Studying Protein Folding

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The path to solving the protein folding problem.

Jenny Straiton1

  • 1Contributing Editor.

Biotechniques
|June 12, 2023
PubMed
Summary
This summary is machine-generated.

Artificial intelligence and advanced imaging may have solved the protein folding problem. This breakthrough could accelerate drug discovery and our understanding of biological processes.

Keywords:
AlphaFoldAlphaFold2artificial intelligencecryo-EMcryogenicscrystallographydeep learning

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Area of Science:

  • Computational biology and structural biology.
  • Artificial intelligence and machine learning applications in bioinformatics.
  • Advanced biomedical imaging techniques.

Background:

  • The protein folding problem, a grand challenge in science, concerns predicting a protein's three-dimensional structure from its amino acid sequence.
  • Traditionally, experimental methods like X-ray crystallography and cryo-electron microscopy were used, but these are time-consuming and resource-intensive.
  • Recent progress in artificial intelligence, particularly deep learning, has shown remarkable promise in predicting protein structures with unprecedented accuracy.

Discussion:

  • The integration of artificial intelligence (AI) with novel imaging technologies represents a paradigm shift in structural biology.
  • AI algorithms can now predict protein structures with accuracy comparable to experimental methods, significantly reducing the time and cost.
  • This advancement has profound implications for understanding protein function, disease mechanisms, and drug development.

Key Insights:

  • AI-powered predictive software, combined with enhanced imaging, is rapidly advancing the solution to the protein folding problem.
  • The accuracy and speed of these computational methods are revolutionizing structural biology research.
  • This convergence of technologies offers a powerful new toolkit for biological and medical research.

Outlook:

  • The solved or near-solved protein folding problem is expected to accelerate the design of novel therapeutics and enzymes.
  • Further integration of AI will likely lead to breakthroughs in understanding complex biological systems and disease pathways.
  • Continued advancements in computational power and algorithms will further refine protein structure prediction and design capabilities.