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Structure of enzyme protiens, and how they fulfill their biological role

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My problem is as follows. I need to write a short account of no more than 400 words in which I discuss:-

The general stucure of enzyme protiens, and

how the stucture of enzymes allows them to fulfill their biological role.

I am to include the following terms into the above account:-
Primary Stucture
Peptide bonds
Weak Bonds
Higher-order Stucture
Globular protien
Energy barrier
Active site
Enzyme-substrate complex

I know all the terms are their and can be easily looked up, I am having trouble trying to put things in order and keep within the word limit. Can anyone please help me with this

Thank you

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You can start by explaining the basic components of proteins: amino acids, an acidic carboxyl group and a side chain (R) attached to a carbon atom.
<br><br><br>Twenty kinds of amino acids enter the makeup of proteins during biologic synthesis. This takes place on the ribosomes under the direction of messenger RNA, which in turn is under genetic control. Several modifications of the 20 amino acids may take place subsequently, so that 23 or more kinds of amino acids are found in plants, and animals synthesize some.
<br><br><br>All protein molecules are long chains of amino acids joined by peptide linkages or bonds. Two amino acids joined together form a dipeptide and many more of these amino acids being joined together form many polypeptides. Long polypeptide chains are called "proteins". Proteins and the properties associated with them are the result of more than just the sequence of amino acids. For this reason, several levels of organization are recognized:
<br><br><br>1. Primary structure - made up of the kind and sequence of amino acids in a protein.
<br><br><br>2. Secondary structure - this is the alpha helix , which is a spiral form maintained by weak hydrogen bonds between the carboxyl group of one amino acid and the amino group of an adjacent one in the helix.
<br><br><br> Globular proteins contain varying amounts of alpha-helix and beta-pleated sheets folded into higher levels of structure or higher order structure called the:
<br><br><br>3. Tertiary structure- this is the three dimensional form of the protein, which is maintained by strong and weak bonds between certain amino acids in the folded chains. Bonds which maintain this structure include disulfide bonds, covalent bonds and hydrogen bonds.
<br><br><br>Some proteins are composed of more than one peptide. The noncovalently bound subunits of these proteins are the quaternary structure. The forces that maintain tertiary and quaternary structure are a variety of weak interactions between the R groups of the constituent amino acids.
<br><br><br> Proteins are the "work horses" of the cell. They serve as enzymes, biological catalysts that increase the rate of metabolic reactions to the speed required to maintain life.
<br><br><br>Enzymes are the biological catalysts of cell. They lower the activation energies, but do not alter the equilibrium constants of the reactions they catalyze. Enzymes are classified according to function. The six general classes include oxireductases, transferases, hydrolases, lyases, isomerases and ligases. Enzymes are also classified on the basis of their ...

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