unit 2 – chemistry of life
TRANSCRIPT
ProteinsUnit 2 – Chemistry of Life
Proteins
http://www.youtube.com/watch?v=g9G0zzdQx-M&feature=related
Contain: Carbon, hydrogen, oxygen, nitrogen, and
sometimes sulfur Form the basic structure of many
animal parts, such as muscle, skin, hair, and bone.
Enzymes are also proteins.
Proteins
Are formed from amino acids:
On the left: amine group On the right: carboxyl group “R” represents an atom or group of atoms
which varies with each different amino acid.
Proteins
20 different amino acids form proteins
They join by dehydration synthesis:
Polypeptides
Two or more amino acids bonded together are called a peptide.
A chain of many amino acids is referred to as a polypeptide. The complete product, either one or more chains of amino acids, is called a protein.
There is unequal sharing of electrons in a peptide bond. The O and the N are negative and the H is positive.
Levels of Structure
Protein structure is described in 4 levels: 1. Primary structure 2. Secondary structure 3. Tertiary structure 4. Quaternary structure
Primary Structure
Is a chain of amino acids joined by dehydration synthesis and held together by peptide bonds (strong covalent bonds: C-N)
Organized in linear arrangements E.g. Cow insulin
Primary Structure
Proteins differ in 3 ways: 1. number of amino acids in the chain 2. types of amino acids 3. sequence of amino acids
Each different sequence is a different protein
Primary chains are 51 to thousands of amino acids long
There is an infinite number of different proteins
Secondary Structure
The straight primary chain of amino acids spontaneously coils, forming hydrogen bonds between amino acids.
Eg. Alpha-helix (hair)
hydrogen bonds
Secondary proteins are structural proteins (e.g. hair, cartilage) and are insoluble in water
Tertiary Structure
“Globs” Interactions (hydrogen bonds)
between R-groups of the amino acids hold these proteins in a 3-dimensional globular shape.
The specific globular shape is essential for the proteins of biological function.
Tertiary Structure
Primary chain of amino acids held together by peptide bond
Hydrogen bonds between some R-groups (weak bonds)
Quaternary Structure
Large globular proteins formed when 2 or more tertiary (globular) proteins join
E.g. hemoglobin – 4 globular proteins
Denaturation of Proteins
Globular proteins can easily be denatured.
For example, the hydrogen bonds holding the protein in its 3D shape are broken by acid, base, change in pH, or heat and the protein reverts back to its primary structure (chain of amino acids).
Denaturation
3D primary chain
The protein loses its biological function since its 3D shape is essential for it to function.
Once the heat, acid or base is removed, the protein may go back to its tertiary shape and resume its biological function.
Coagulation
A permanent change in protein shape caused by too much heat, acid, or base.
“Permanent denaturation” E.g. boiling an egg: no matter how
long the egg cools, the proteins of the egg will never assume their original shape
Hydrolysis of Protein
Hydrolysis of Protein
Hydrolysis is the reverse reaction to dehydration synthesis
Proteins you eat are hydrolyzed during digestion
Hydrolysis breaks the peptide bonds i.e. destroys the primary structure
Protein + many water molecules amino acids
Proteins
Video Intro for Protein Lab: http://www.youtube.com/watch?v=w-ctk
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Video closure for Protein Lab http://www.wisc-online.com/Objects/View
Object.aspx?ID=BIC007