1) What are the four levels of protein folding. How do you distinguish those different levels? What can denature a protein? 2) What are detergents and why are they useful? How do they basically work? 3) What is meant by amphipathic? What is an example of this?
Proteins
We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.
Protein Expression
The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.
1) What are the four levels of protein folding. How do you distinguish those different levels? What can denature a protein?
2) What are detergents and why are they useful? How do they basically work?
3) What is meant by amphipathic? What is an example of this?
The proteins are macromolecules that have important functions in the biological activity. The amino acids are the building blocks of the protein; the amino acids are the small molecules that bind together to form a complex macromolecule called protein. The amino acids are important for many functions like cell structure, cell repair, forming of connective tissue and skin, and muscle. The protein is a three dimensional of amino acids that form a chain molecule. The proteins are polymers that are formed by the sequences of amino acids that fold according to the specific types of amino acids.
The four stages of protein folding are primary, secondary, tertiary, and quaternary.
- The primary stage of protein folding is held by peptide bonds
- The secondary stage of protein folding has alpha-helix and beta-pleated sheets. The alpha helix is bonded by hydrogen bonds in the same direction of the protein fold. The beta-pleated sheet has an S-shape pattern that is held by hydrogen bonds that gives structure.
- The tertiary stage of protein fold is a 3D structure that takes part in the function, and held by non-covalent bonds. The non-covalent bonds will also have interaction with side groups such as hydrophobic interaction, ionic interaction, hydrogen bonds, Van der Waals forces, and disulfide bonds.
- The quaternary stage of the protein fold, the single peptides bonds are bond by other peptides.
- Protein is denatured when the quaternary structure is lost. Heat and alcohol are considered to have a major impact on the quaternary structure.
The detergents have long molecules that have head and tail. The long molecules of the detergents are also called as surfactants, where the head is hydrophilic and the tail is hydrophobic. The head of the detergents attracted to the water, while tail being hydrophobic will attract grease. The detergents were useful in the lysis of cells and the splitting of molecules.
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