Biokimia: Asam Amino dan Protein

Updated: 6/6/2024


Summary

Amino acids are the monomers that make up proteins, consisting of a carboxyl group, an amine group, and a side chain. There are 20 different amino acids used in proteins, differing in their side chains. Amino acids can be grouped based on their side chains into nonpolar aliphatic, polar neutral, negatively charged, positively charged, and aromatic. They can also be classified as essential (required from diet) or non-essential (synthesized by the body). Amino acids have optical isomers, can form zwitterions, act as acids and bases, and have an isoelectric pH. Peptides are formed by linking two or more amino acids via peptide bonds, with different nomenclature based on the number of amino acids. Peptides have various functions like hormones and toxins. Proteins have four structural levels: primary (amino acid sequence), secondary (alpha helices and beta sheets), tertiary (overall 3D folding), and quaternary (multiple polypeptide chains). Proteins are classified by function as enzymes, nutrients/storage, structural, defense, contractile, transport, or regulatory, and by shape as globular or fibrous. The structure and properties of amino acids and proteins are crucial for understanding their roles in biological processes.

Introduction to Amino Acids

Amino acids are the monomers that make up proteins. They consist of a carboxyl group, an amine group, and a side chain. There are 20 different amino acids used in proteins, differing in their side chains.

Structure of Amino Acids

The general structure of amino acids includes a carboxyl group (COOH), an amine group (NH3), and a side chain (R). The 20 amino acids can be grouped based on their side chains: nonpolar aliphatic, polar neutral, negatively charged, positively charged, and aromatic.

Properties of Amino Acids

Amino acids have several properties: they are optically active, forming L and D isomers; they can exist as zwitterions (both positive and negative ions); they can act as acids and bases; and they have an isoelectric pH.

Peptides

Peptides are formed by linking two or more amino acids through peptide bonds. They are named based on the number of amino acids (dipeptide, tripeptide, etc.) and the sequence of amino acids from the N-terminus to the C-terminus.

Functions of Peptides

Peptides have various functions, such as hormones (e.g., insulin, glucagon) and toxins (bioactive peptides).

Protein Structure

Proteins have four levels of structure: primary (sequence of amino acids), secondary (alpha helices and beta sheets), tertiary (3D folding), and quaternary (multiple polypeptide chains).

Classification of Proteins

Proteins can be classified based on their functions (enzymes, nutrients, structural, defense, activators, transport, regulatory) and their shapes (globular or fibrous).


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FAQ

Q: What are the monomers that make up proteins?

Amino acids are the monomers that make up proteins.

Q: How many different amino acids are used to make proteins?

Only 20 different amino acids are used to make proteins.

Q: What are the four levels of protein structure?

The four levels of protein structure are primary, secondary, tertiary, and quaternary.

Q: What is the difference between primary and secondary protein structure?

Primary structure refers to the sequence of amino acids, while secondary structure refers to the three-dimensional structure resulting from hydrogen bonding between amino acids.

Q: How are proteins classified according to their function?

Proteins are classified into seven groups according to their function: enzymes, nutrients and storage, structural, defense, activator or contractile, transport, and regulatory.