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Related Concept Videos

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...
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
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
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...
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...

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Related Experiment Video

Updated: Jun 13, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Stabilization of proteins for storage.

Richard J Simpson

    Cold Spring Harbor Protocols
    |May 5, 2010
    PubMed
    Summary

    Maintaining protein stability during long-term storage is crucial for proteomics research and pharmaceutical applications. Proper storage conditions, including temperature, pH, and additives like glycerol, are essential to prevent protein inactivation and aggregation.

    Area of Science:

    • Biochemistry
    • Proteomics
    • Pharmaceutical Science

    Background:

    • Proteins and peptides require long-term storage after purification for subsequent analyses.
    • Maintaining biological function and preventing inactivation are critical for protein pharmaceuticals and research samples.
    • Protein shelf-life is influenced by intrinsic properties and extrinsic storage conditions.

    Purpose of the Study:

    • To discuss major causes of protein inactivation.
    • To describe measures for maintaining protein stability and solubility during storage.

    Main Methods:

    • Review of factors affecting protein stability.
    • Discussion of storage conditions (temperature, pH).
    • Exploration of stabilizing additives (e.g., glycerol, sucrose).

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    Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion (FDAP)
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    Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion (FDAP)

    Published on: January 28, 2015

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    Last Updated: Jun 13, 2026

    How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
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    How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

    Published on: February 11, 2019

    Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
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    Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

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    Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion (FDAP)
    09:45

    Measuring Protein Stability in Living Zebrafish Embryos Using Fluorescence Decay After Photoconversion (FDAP)

    Published on: January 28, 2015

    Main Results:

    • Protein inactivation is caused by various intrinsic and extrinsic factors.
    • Appropriate storage conditions are vital for preserving protein activity.
    • Additives like glycerol and sucrose can prevent aggregation and maintain protein function.

    Conclusions:

    • Optimal storage strategies are necessary to ensure protein integrity over time.
    • Understanding protein inactivation mechanisms aids in developing effective stabilization methods.
    • Proper handling and storage are key for reliable downstream applications in proteomics and pharmaceuticals.