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1.1.1 Write of the vitamins, a biological role.

Tasteless, organic compounds. Required in small amounts. Functions: ÷Regulate metabolism ÷Help convert energy in fat, carbohydrate, and protein into ATP ÷Promote growth and reproduction. Deficiencies can result in potentially serious consequences

Most metabolic processes in the body require vitamins. Many coenzymes (compounds that help enzymes function in metabolic processes) are composed of vitamins.

Vitamin Structure and Function All vitamins contain carbon, hydrogen, and oxygen. Some vitamins contain nitrogen and sulfur. Chemical structure of each vitamin is unique. Each vitamin is a singular unit. Vitamins are absorbed intact. Vitamins perform numerous essential functions

Each new vitamin is temporarily named when discovered. The naming of vitamins follows the letters of the alphabet, starting with A; we are up to the letter K

A, B, C, D, E, and K, B has many subscripts, F, G, and H were dropped

There are 13 different vitamins, each with its own special roles. Vitamins are grouped into two major categories; fat-soluble vitamins and water-soluble vitamins.

Fat-soluble vitamins (4 fat soluble) Vitamin A Vitamin D Vitamin E Vitamin K

Water-soluble vitamins (9 water soluble: 8 B vitamins & C) ÷Thiamin ÷Riboflavin ÷ Niacin ÷Biotin ÷Pantothenic acid ÷ Vitamin B6 ÷Folate ÷ Vitamin B12 ÷Vitamin C

1.1.2 Write the basic structure of proteins.

Protein structure describes how protein molecules are organised. This structure is what makes proteins work.

Proteins are important biological macromolecules present in all organisms. They are polymers formed from 20 possible amino acids by RNA translation. Protein structures range in size from tens to several thousand amino acids.

After translation, proteins fold into specific shapes. This is not done by chemical bonds but by weaker forces such as hydrogen bonds. To understand how proteins work, it is often necessary to discover their three-dimensional structure. To do this biophysics uses techniques such as X-ray crystallography, NMR spectroscopy, and dual polarisation interferometry.

A protein may switch from one shape to another as it does its job. The alternative states of the same protein are called conformations. An enzyme, for instance, will have at least two conformations: one with its co-enzyme and one without. The form with its coenzyme will have two conformations: one with its substrate and one without.

1.1.3 Write the secondary and tertiary protein structures.

Secondary structure

An alpha-helix with hydrogen bonds (yellow dots)

Secondary structure refers to highly regular local sub-structures. Two main types of secondary structure, the alpha helix and the beta strand (beta sheet), were suggested in 1951 by Linus Pauling and coworkers. These secondary structures are defined by patterns of hydrogen bonds between the main-chain peptide groups.

Tertiary structure

This is the shape (spatial organization) of an entire protein molecule. Protein folding is largely self-organising. It is mainly done by the protein's primary structure – its sequence of amino acids. This is called Anfinsen's dogma. However, the environment in which a protein is synthesized and folds also effect its final shape.

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