Proteins Ms Glasgow.

Slides:



Advertisements
Similar presentations
Carbohydrates, Lipids, Proteins, and Nucleic Acids
Advertisements

Proteins are all made from chains of amino acids.
Protein Structure & Function
Welcome to class of Amino Acids Dr. Meera Kaur. Learning objectives To understand - the structural features of amino acids - the classifications of amino.
Lesson 5.  Explain the term secondary structure  Explain the term tertiary structure.
Peptides and Proteins 20 amino acids are commonly found in protein. These 20 amino acids are linked together through "peptide bond" forming peptides and.
LESSON 1-3: Biomacromolecules LEARNING OUTCOMES By the end of these lessons, you should be able to: Describe the structure and function of lipids. Describe.
INB PG 17 CHAPTER 2.4: PROTEINS. PROTEINS Composed of monomers called amino acids Extremely important macromolecule More than 50% dry mass of cell is.
19.1 Proteins and Amino Acids
Proteins Major group of biological molecules. Proteins Monomers: amino acids ▫Always contain an amino group and carboxylic acid group Polymers: peptides.
Chapter 19 Amino Acids and Proteins
Topic 7.5 Proteins (AHL).
Hannah Barreca Daria Lukasz Ian Reucroft Roshelle Belfer Stephanie Puthumana.
BRANDI AND ZAK. Secondary Structure Can fold and align them selves and the repeating pattern is called a secondary structure. Common structures are the.
Peptides and Proteins 20 amino acids are commonly found in protein. These 20 amino acids are linked together through "peptide bond" forming peptides and.
Chapter 14 Proteins Chemistry 20. Function of proteins Fibrinogen helps blood clotting.
PROTEINS C, H, O, N, (S) Polymers made from chains of amino acids 20 amino acids used Linked by a peptide bond.
Amino acids. Essential Amino Acids 10 amino acids not synthesized by the body arg, his, ile, leu, lys, met, phe, thr, trp, val Must obtain from the diet.
-OH  Name of Functional group: This is a hydroxyl  Function of the group: Draws electrons  Attracts water, Dissolves organic materials such as sugar.
THE STRUCTURE AND FUNCTION OF MACROMOLECULES Proteins - Many Structures, Many Functions 1.A polypeptide is a polymer of amino acids connected to a specific.
P ROTEINS SBI4U Ms. Manning. Most diverse molecules in living organisms. Coded for by genes in the DNA Used as: Structural building blocks Catalysis -
©1999 Timothy G. Standish Bielkoviny, enzýmy Protein Structure Július Cirák.
Chapter 2.4: Proteins.
The Structure of Proteins. Functions of Proteins Fibrous proteins – structural, e.g. collagen. Globular proteins – metabolic functions, e.g. haemoglobin.
Aim: What is the primary structure of proteins ?.
Protein- Secondary, Tertiary, and Quaternary Structure.
Amino Acids, Peptides, and Proteins. Introduction to Amino Acids  There are about 26 amino acids, many others are also known from a variety of sources.
Protein Recap. Protein Syllabus Draw the general amino acid structure.
DO NOW 10/18 WOD: DETER (di TUR) v. to discourage; to keep someone from doing something DO NOW: Please prepare yourselves for a (quick) quiz on water!
Lesson starter What three elements are common to fats, carbohydrates and proteins? What reaction unites single units of fats, carbohydrates and proteins?
PROTEINS Have a wide range of functions; haemoglobin, antibodies & enzymes Amino acids are the monomers Twenty naturally occurring amino acids The order.
Module Biological Molecules Proteins By Ms Cullen.
Biological Molecules: Proteins  Links to GCSE  Bonding  Balanced diet & food tests  Hormones & immunity  Haemoglobin.
Denaturation of proteins Some of the interactions responsible for holding a protein in its 3D tertiary structure are weak –Eg hydrogen bonds They are easily.
Protein Structure.
Lesson 6.  Textbooks  Repro  Page 8-9 of ppq  Comparison sheet.
7.3 Protein structure This could be you!. Secondary Structure.
The Structure and Function of Macromolecules. II. Classes of Organic Molecules: What are the four classes of organic molecules?
© SSER Ltd.. Proteins are huge three-dimensional molecules whose building blocks or monomers are the variety of different amino acids found in nature.
Protein chemistry Lecture Amino acids are the basic structural units of proteins consisting of: - Amino group, (-NH2) - Carboxyl group(-COOH)
Biology Induction.
Proteins What do we need proteins for?
© SSER Ltd..
Proteins have a very wide range of functions in living organisms.
Proteins Part 2 Review of protein structure, Types of Proteins, Testing for Proteins.
Proteins Red hunting B1.3 - Explain how the structure of collagen and haemoglobin are related to their function.
Amino Acids, Proteins, and Enzymes
Proteins: Secondary and Tertiary Structure
Protein Structure Amino Acids Polypeptide Levels of Structure
Proteins.
Biomacromolecules Part IV: Proteins.
Chapter 2.4: Proteins.
Conformationally changed Stability
Proteins.
Proteins.
Proteins Haileybury Astana IB SL Biology.
The Chemistry of Life Proteins
Proteins.
Amino acids R-groups non-polar polar acidic basic proteins
Chapter 19: Proteins.
What is they, what makes them etc
Amino acids R-groups non-polar polar acidic basic proteins
Conformationally changed Stability
PROTEINS FOLDED POLYPEPTIDES.
Worked Example Determining Side-Chain Hydrophobicity/ Hydrophilicity
Presentation transcript:

Proteins Ms Glasgow

Proteins- gps of organic compounds consisting of C, H, O & Sometimes S The monomer is an amino acid The amino acid has a chiral carbon

Peptide Bonding

Categories of Amino Acids

What happens when amino acids reacts with water? Answer: Zwitterion formed (contains separate parts which are +vely & - vely charged) Reason: Internal transfer of a hydrogen ion from the -COOH group to the -NH2 group -> ion with both a -ve charge & a +ive charge In acidic solutions:  The -COO- part of the zwitterion picks up a hydrogen ion, resulting in a +vely charged amino acid (Left) In basic solutions: The hydrogen ion is removed from the -NH3+group, resulting in a –vely charged amino acid (right) Conclusion: The zwitterion acts as a pH buffer ( able to resist changes in the pH of its surrounding)

Hydrogen Bonds Formed between R groups w/h are dipoles e.g carboxyl, hydroxyl & amino groups Relatively weak bonds

Ionic Bonds Formed between groups with opposite charge e.g ionised carboxyl and amino groups Bond is stronger than H- bonds

Disulphide Bonds Formed between R groups contain S - atoms e.g cysteine Strong covalent bonds due to oxidation of 2 S – atoms by dehydrogenation

Hydrophobic Interactions Formed with non-polar R groups e.g. tyrosine & valine In aq. Sol’n -> hydrophobic group gathers in the interior away from water while hydrophilic group forms an outer shield towards the water

Protein Structure

Haemoglobin (Globular Protein) Carries O2 in RBC Consists of 4 separate polypeptides 2 alpha (141 aa) & 2 beta chains (146 aa) 1 haem gp with 1 O2 per chain Soluble in water re: hydrophobic side gp inward but hydrophilic side gp outward towards water Sickle cell anaemia <- mutation <- hydrophilic R group is replaced by a hydrophobic R group

Collagen (Fibrous Protein) Component of connective tissues such as tendons & blood vessels & binds inorganic crystals Consists of 3 polypeptide chains Each chain of repetitions of 3 aa (proline, glycine, alanine) Insoluble in water re: long (1000 aa) & hydrophobic R gps Assemble into flexible fibres w/h cannot stretch

Food test

Reducing Sugars

Non-reducing Sugars

Starch

Protein

Lipids