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Chemistry · Ch 14 — Biomolecules

Denaturation of Proteins

14.2.7

Denaturation of Proteins

Each protein has a unique three-dimensional structure held together by interactions such as disulphide bonds, hydrogen bonds, and hydrophobic and electrostatic interactions. These stabilising interactions can be disturbed when the protein is exposed to higher temperature, to certain chemicals such as urea, or to a change in pH or ionic strength, and this disturbance leads to a partial or complete loss of the protein's three-dimensional (higher-order) structure. This process -- losing the higher-order structure while the primary structure (the amino-acid sequence itself) stays intact -- is called denaturation. When a protein denatures, its biological function is lost along with its shape. …

Figure 14.18Denaturation of proteins

What this figure shows. A before/after schematic contrasting a native, compactly folded globular protein on one side with its denatured form on the other -- an unfolded, disordered tangle of the same polypeptide chain with its secondary and tertiary structure lost -- captioned with the coagulation of egg white by heat as the everyd …