As amino acids are added to a polypeptide during translation, tRNA molecules will enter the A site of the ribosome. The tRNA is then transferred to the P site, where a peptide bond is formed between the amino acid residue and the amino acid chain. Finally, the tRNA moves to the E site to release its tRNA and exit the ribosome.

As amino acids are added to a polypeptide during translation, tRNA molecules will enter the A site of the ribosome. The tRNA is then transferred to the P site, where a peptide bond is formed between the amino acid residue and the amino acid chain. Finally, the tRNA moves to the E site to release its tRNA and exit the ribosome.

As amino acids are added to a polypeptide during translation, tRNA molecules will enter the A site of the ribosome. The tRNA is then transferred to the P site, where a peptide bond is formed between the amino acid residue and the amino acid chain. Finally, the tRNA moves to the E site to release its tRNA and exit the ribosome.

Pepsin is an enzyme in the stomach that digests proteins. Because it is active in the stomach, which is highly acidic, pepsin best functions at a low pH between 2 and 2.5.

Pepsinogen is secreted by chief cells and converted into active pepsin after catalyzation by hydrochloric acid. The acid is secreted by parietal cells in response to gastrin secretion by G cells. After the stomach contents enter the duodenum of the small intestine, the acid is neutralized by bicarbonate secretions from the pancreas. This prevents the acid from damaging the walls of the small intestine.

Proteins have the most diverse functions in biological systems. Their remarkable diversity in function is due to their diversity in structure. Structural proteins, such as tubulin and collagen, have a fibrous structure that aids their function. Enzymes have active sites that allow them to bind specific molecules (substrates) and enact a conformational change to facilitate chemical reactions. Signaling proteins include several types of hormones, known as peptide hormones. Protein receptors are commonly found embedded in the cell membrane and contain active sites to bind substrates, hydrophilic regions to interact with the cell environment and extracellular space, and hydrophobic regions to interact within the lipid bilayer.

Ribosomes are responsible for translating mRNA into protein. tRNA molecules transport amino acids to the ribosome, where they are joined by peptide bonds to form a chain. This chain of amino acids is known as the protein primary structure.

Secondary structure, tertiary structure, and quaternary structure form in the cytoplasm or endoplasmic reticulum after the ribosome has released the polypeptide.

Proteins have the most diverse functions in biological systems. Their remarkable diversity in function is due to their diversity in structure. Structural proteins, such as tubulin and collagen, have a fibrous structure that aids their function. Enzymes have active sites that allow them to bind specific molecules (substrates) and enact a conformational change to facilitate chemical reactions. Signaling proteins include several types of hormones, known as peptide hormones. Protein receptors are commonly found embedded in the cell membrane and contain active sites to bind substrates, hydrophilic regions to interact with the cell environment and extracellular space, and hydrophobic regions to interact within the lipid bilayer.

Inhibitors are able to prevent maximum enzymatic rates in a variety of ways. Some inhibitors, like noncompetive inhibitors, are able to attach at a point on the enzyme and alter its conformation. Competitive inhibitors, however, bind directly at the active site, which prevents substrate from entering the enzyme.

Competitive inhibitors are the only inhibitor type to bind directly to the enzyme actve site.

Pepsin is an enzyme in the stomach that digests proteins. Because it is active in the stomach, which is highly acidic, pepsin best functions at a low pH between 2 and 2.5.

Pepsinogen is secreted by chief cells and converted into active pepsin after catalyzation by hydrochloric acid. The acid is secreted by parietal cells in response to gastrin secretion by G cells. After the stomach contents enter the duodenum of the small intestine, the acid is neutralized by bicarbonate secretions from the pancreas. This prevents the acid from damaging the walls of the small intestine.

Inhibitors are able to prevent maximum enzymatic rates in a variety of ways. Some inhibitors, like noncompetive inhibitors, are able to attach at a point on the enzyme and alter its conformation. Competitive inhibitors, however, bind directly at the active site, which prevents substrate from entering the enzyme.

Competitive inhibitors are the only inhibitor type to bind directly to the enzyme actve site.