Protein structure and molecular biology

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Protein molecular structure

DP Biology

Proteins

Illustration of protein structure

Proteins are very important molecules in all living things. There are different types and functions that a protein can perform.

For example, proteins can: build the structure of the cell, break down molecules, and make the reactions happen faster. Each protein is made of smaller units called amino acids. These terms will take a closer in-depth look at some of the proteins that are important to the function of each cell.

What Are Proteins?

Proteins are the macromolecules of the cell. Proteins and other macromolecules of the cell are formed from a series of smaller units that are called monomers.

Amino Acids

Each of the cell's proteins is made of long chains of monomers called amino acids.

When a long chain of these monomers is formed, that is referred to as a polypeptide.

Each protein is built according to a set of instructions that is found in the DNA of the cell. That is why the proteins that are made in each cell are made just for that cell.

Amino Acids - Proteins

Amino acids play the role of the structural components of proteins.

There are three parts to an amino acid:

  • An amino group
  • A carboxyl group
  • A side chain (R group)

While the amino and carboxyl groups are constant, the R group differs with each amino acid, which gives each amino acid distinct chemical properties.

Of the twenty amino acids, some are basic, some are polar, some are non-polar, some are acidic, and others are basic.

Peptide Bonds - Protein Formation

Amino acids are joined together through a chemical bond called a peptide bond. Typically, a peptide bond forms when the carboxyl group of one amino acid interacts with the amine group of another amino acid, and a molecule of water is released. This is identified as a condensation reaction.

  • A dipeptide is formed when two amino acids are linked
  • A polypeptide is formed when many amino acids are linked

A polypeptide chain that has folded to achieve the desired conformation is a functional protein.

Protein Structure Levels

A protein has a total of four structural levels, and each of these levels contributes to the overall shape and function of the protein.

1. Primary Structure

The primary structure of the protein is composed of the total number of amino acids arranged in a chain that forms a polypeptide. This sequence is dictated by the organism's DNA.

For instance: A single amino acid substitution in the hemoglobin of an individual is responsible for the occurrence of sickle cell anemia.

2. Secondary Structure

The secondary structure of a protein is its folding of polypeptide chains into alpha helices and beta-pleated sheets.

The secondary structure is stabilized by hydrogen bonds formed between the backbone (protein backbone) atoms.

Example: An alpha helix structure in keratin and beta sheets in silk fibroin.

3. Tertiary Structure

The tertiary structure is the 3D folding of a polypeptide chain.

The tertiary structure is stabilized by:

  • Hydrogen bonds
  • Ionic bonds
  • Disulfide bridges (the covalent bond between two cysteine residues)
  • Hydrophobic interactions

Example: Myoglobin has a compact globular structure.

4. Quaternary Structure

This occurs when more than one polypeptide chain assembles to form a functional protein.

The quaternary structure is stabilized by the same bonds as the tertiary structure.

Example: Hemoglobin has 4 subunits.

The Functions of Proteins

Proteins are highly versatile molecules with multiple functions.

Structural Proteins

These provide the support and structure to the cells and tissues.

Example: Collagen (connective tissue) and keratin (hair and nails).

Enzymes

These are biological catalysts that speed up chemical reactions and are not consumed in the process.

Example: Amylase is an enzyme that breaks down starch into glucose.

Enzymes are highly specific to the substrates they act upon (due to the 'active site' on the enzyme).

Transport Proteins

These proteins facilitate the transport of molecules across membranes and throughout the blood.

Example: Hemoglobin (carries oxygen) and channel proteins (allow and facilitate the movement of specific ions).

Hormonal Proteins

These are chemical messengers that control and regulate physiological activity.

Example: Insulin is a protein that regulates the level of glucose (sugar) present in the blood.

Defensive Proteins

These are proteins that protect the body from foreign particles or substances.

Example: Antibodies are specific proteins that attach (bind) to antigens to neutralize pathogens.

Storage Proteins

Proteins that serve to store nutrients and energy in the body.

Example: Ferritin is an example of a storage protein that stores iron.

Denaturation of Proteins

Denaturation refers to the loss of structure and hence function of a protein. Denaturation involves the loss of secondary, tertiary, and quaternary structure, but primary structure remains unchanged.

Denaturation can occur due to:

  • Heat: breaks hydrogen bonds
  • Changes in pH: can disrupt ionic bonds
  • Chemicals: such as urea, detergents, and heavy metals can alter the way proteins are folded

Example: Cooking an egg is an example of denaturation. Clear egg white is transformed into white because of denatured ovalbumin.

Enzyme Function - A Special Case of Proteins

Enzymes are a type of globular protein that catalyze biochemical reactions. The function of enzymes is determined by their shape.

Key Concepts:

  • Active Site: The area where a substrate binds.
  • Substrate Specificity: Only one substrate can fit into an enzyme.
  • Induced Fit: The enzyme will change its shape slightly to fit the substrate better.

What Affects Enzyme Activity?

Factors Affecting Activity

  • Temperature: Each enzyme has an optimal temperature. Too much heat can denature the enzyme.
  • pH: Each enzyme has an optimal pH.
  • Substrate concentration: Higher concentration increases the rate of the reaction until saturation is reached.
  • Inhibitors: These are molecules that lessen the activity of the enzyme.

Types of Inhibition

  • Competitive Inhibition: The inhibitor competes with the substrate to bind with the active site.
  • Non-competitive Inhibition: The inhibitor binds to an area that is not the active site and alters the shape of the enzyme.

Protein Synthesis - From DNA to Functional Protein

Protein synthesis can be divided into two main steps: transcription and translation.

Transcription

  • In the nucleus, DNA is used to make a copy of mRNA.
  • RNA polymerase reads the DNA and synthesizes the complementary strand.

Translation

  • The ribosome is where the mRNA will attach.
  • tRNA is responsible for bringing the amino acids that are complementary to the codons of the mRNA.
  • The amino acids will be linked together by peptide bonds to create a polypeptide, which will then fold into its functional state.

Nucleotides in a DNA strand create a specific protein sequence by determining a specific order of amino acids, which then creates a defined protein function and structure.

Summary

  • A long strand of amino acids results in a protein via a process called a peptide bond.
  • A protein can have four levels of structure: primary, secondary, tertiary, and quaternary.
  • Shelves, enzymes, transport, hormone production, defense, and storage are functions that can be performed by proteins.
  • An enzyme can be denatured, meaning that its function is disrupted, without its peptide bonds breaking.
  • Enzymes are a type of specialized protein that catalyze a reaction, and can be impacted by temperature, pH, and certain inhibitors.
  • Transcription (the process of DNA being converted to RNA) and translation (the process of RNA being converted into a protein) are the two steps of protein synthesis.
  • Every protein malfunction can potentially cause a disease, and there are many reasons to study proteins, including the fact that proteins control nearly all of the functions of a single cell in an organism. They are more than just building blocks of cell structures. Proteins are the cell's defenders, its signals, and its machinery.