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Modalites of protein denaturation - Coggle Diagram
Modalites of protein denaturation
Diagrammatic representation of protein
denaturation using GdmCl and Urea as denaturants
Denaturation
bio-chemical process which can be defined as any alteration in secondary structure, tertiary structure or the quaternary structure of protein molecule which results in disruption of covalent bonds
Almost all of the proteins known to exist, in their native states, are folded into well-defined and are usually essentially rigid and possess three-dimensional structures
Reduced solubility
The process of protein denaturation is often accompanied by denatured protein precipitation through the addition of smaller amounts of neutral salts
Increased constituent group reactivity
alterations in the chemical nature accompany the denaturation of the protein
Depletion of crystallizing property
globular proteins which are capable for crystal formation
Decrease in biological activity
biochemical activities of the proteins or enzymes may get destroyed due to denaturation
Alteration in shape of protein molecule
Protein molecules in their native state are equipped with specific molecular dimensions which are expressed as shape and size
Susceptibility to enzymatic hydrolysis
A denatured or unfolded protein molecule can be easily digested as compared to native state of the protein by enzymes like proteinases, which attack peptide bonds
Denaturation Degree
Characterization of protein molecule is done by considering its amino acid composition and physical configuration
