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Protein Denaturation01:28

Protein Denaturation

4.4K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
4.4K
Protein Folding01:25

Protein Folding

8.1K
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...
8.1K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

40
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...
40
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

12.4K
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...
12.4K
Drying Shrinkage01:21

Drying Shrinkage

108
When hardened concrete is exposed to air with a relative humidity of less than 100 percent, it begins to lose the free water within its capillaries. As this water evaporates, the water initially adsorbed onto the calcium silicate hydrates migrates towards these now empty spaces and eventually evaporates as well. Over time, as more water leaves, the volume of the concrete decreases, a phenomenon known as drying shrinkage.
A portion of this drying shrinkage can be reversed; if the concrete is...
108
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.1K
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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Related Experiment Video

Updated: Jul 26, 2025

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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Chemical Changes Over Time Associated with Protein Drying.

Allan Kimble, Christopher Ratanski, Terra A Kremer

    Biomedical Instrumentation & Technology
    |June 21, 2023
    PubMed
    Summary
    This summary is machine-generated.

    Drying proteins causes changes in molecular weight due to oligomerization and degradation. Understanding these chemical changes is crucial for cleaning medical devices and preventing retained surgical soils.

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    Area of Science:

    • Biochemistry
    • Materials Science

    Background:

    • Protein coagulation during drying is not well understood.
    • Changes in protein structure affect medical device cleanability.
    • Understanding protein drying chemistry is essential for mitigating retained surgical soils.

    Purpose of the Study:

    • To investigate the chemical phenomena of protein drying.
    • To characterize the changes in protein molecular weight distribution upon drying.

    Main Methods:

    • High-performance gel permeation chromatography (HPGPC).
    • Right-angle light-scattering detection at 90°.

    Main Results:

    • Drying altered protein molecular weight distribution towards higher values.
    • Observed changes attributed to oligomerization, degradation, and entanglement.
    • Albumin polymerized, decreasing solubility; mucin degraded, releasing polysaccharides.

    Conclusions:

    • Protein drying involves complex chemical changes affecting molecular weight.
    • These findings are critical for developing effective cleaning protocols for medical instruments.