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Proteins.

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Presentation on theme: "Proteins."— Presentation transcript:

1 Proteins

2 Protein Basics Used in variety of cellular functions
leucine valine glycine alanine leucine leucine histi- dine aspara- gine serine proline = Protein A valine leucine glycine alanine leucine leucine histi- dine aspara- gine serine proline = Protein B Amino acids (monomer) leucine valine glycine alanine leucine leucine = Protein C Used in variety of cellular functions Made of smaller amino acids Monomer: Amino acid Polymer: Polypeptide (Protein) Only 20 amino acids… but thousands of proteins Exact arrangement of amino acids determines the protein

3 Amino Acid Structure 5 basic parts 1) Central C atom
2) Amino group (NH2) 3) H 4) Carboxyl group (COOH) 5) R group Only 20 amino acids… Each has different R group

4 What differs between these amino acids?
Notice alanine’s different R group Notice Valine’s different R group R group for glycine Notice leucine’s different R group Notice methionine’s different R group Notice isoleucine’s different R group

5 Enzymes Types of proteins
Enzyme amylase glucose glucose glucose glucose Starch Types of proteins Enzyme: Lowers the energy needed to start chemical reactions ex: Break down food Sensitive to pH, temp ex: If high fever: enzymes lose ability to work Very specific in actions ex: Amylase: Breaks starch into simple sugars Reusable

6 REview Proteins & Enzymes
What are the smaller monomers that make proteins called? How many different amino acids exist? How does each amino acid differ? The NH2 part of the amino acid is called the ____ group. The COOH part of the amino acid is called the ____ group. Which group of proteins help to start chemical reactions? What can cause an enzyme to denature? Explain the lock and key analogy as it relates to enzymes.

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