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Related Concept Videos

RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
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...
RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
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...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Related Experiment Video

Updated: Jul 20, 2026

Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion FDAP
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Review of predicting protein stability changes upon variations.

Yiling Qiu1,2, Tao Huang1, Yu-Dong Cai3

  • 1Bio-Med Big Data Center, CAS Key Laboratory of Computational Biology, Shanghai Institute of Nutrition and Health, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China.

Proteomics
|April 21, 2024
PubMed
Summary

Predicting how genetic variations affect protein stability is crucial for medicine and industry. This review covers computational methods, databases, and experimental techniques for protein stability prediction.

Keywords:
computational methodsdatabasesexperimental approachesmutationsprotein stability

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Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology
  • Bioinformatics

Background:

  • Protein stability is critical for biological function and biotechnological applications.
  • Understanding mutation effects on protein stability is essential for disease research and protein engineering.
  • Accurate prediction of stability changes aids in rational protein design.

Purpose of the Study:

  • To review current computational methods for predicting protein stability changes due to mutations.
  • To survey databases containing protein mutation data and thermodynamic parameters.
  • To discuss experimental techniques for high-throughput assessment of protein stability.

Main Methods:

  • Review of state-of-the-art computational approaches for protein stability prediction.
  • Analysis of features, algorithms, and prediction performance of various computational models.
  • Description of experimental validation methods for computational predictions.

Main Results:

  • Identification and categorization of numerous publicly available databases for protein stability prediction.
  • Detailed overview of computational methods, including their underlying algorithms and predictive accuracy.
  • Summary of experimental techniques suitable for high-throughput stability assessment.

Conclusions:

  • Significant progress has been made in computational protein stability prediction.
  • Challenges remain in improving prediction accuracy and integrating diverse data types.
  • Future research may focus on advanced modeling techniques and experimental-computational integration.