Importance, Characteristics, Structure, Classification, Denaturation.

Slides:



Advertisements
Similar presentations
(carbon-based compounds)
Advertisements

Tertiary Structure of Proteins The tertiary structure defines the specific overall 3-D shape of the protein Tertiary structure is based on various types.
PROTEINS Proteins are the most complex and most diverse group of biological compounds. If you weigh about 70 kg: About 50 of your 70 kg is water. Many.
Protein Structure and Function Review: Fibrous vs. Globular Proteins.
Functional Variety of Proteins Proteins: organic compounds containing carbon (C), hydrogen (H), oxygen (O), nitrogen (N) and sometimes sulphur (S).
Pp 50 – 51 & Pp 15 & Proteins Proteins are polymers of amino acids Each has a unique 3D shape Amino acid sequences vary Proteins are.
Definition: Proteins are macromolecules with a backbone formed by polymerization of amino acids. Proteins carry.
Aeron Perlman Marcos San Martin James Loya Image: explow.com.
Chemistry: An Introduction to General, Organic, and Biological Chemistry, Twelfth Edition© 2015 Pearson Education, Inc Proteins: Secondary, Tertiary,
Chapter 16 Amino Acids, Proteins, and Enzymes
Learning outcomes Describe the structure of an amino acid. Describe the formation and breakage of peptide bonds in the synthesis and hydrolysis of dipeptides.
Organic Nutrients: The Building Blocks of Life 1. Carbohydrates 2.Lipids 3.Proteins 4.Nucleic Acids.
They contain C, H, O, N In some P, S, Mg or Fe are present Proteins are the most diverse biological molecules. They can either function as structral or.
19.6 Primary Structure The primary structure of a protein is the sequence of amino acids in the peptide chain Protein backbone Ala-Leu-Cys-Met.
Protein Structure: Tertiary and Quaternary Structure 20.7 Protein Hydrolysis and Denaturation Chapter 20 Amino Acids and Proteins.
Objectives Identify the structure and function of proteins.
Proteins Structures Primary Structure.
What are proteins? Enzymes Biological catalysts Defense proteins antibodies Transport proteins Hemoglobin or myoglobin Regulatory proteins Insulin or glucagon.
Biomolecules: Nucleic Acids and Proteins
PROTEINS The most complex and multifunctional class of organic molecules Most genes are instructions for making protein molecules Large molecules with.
Carbohydrates, Proteins, Lipids, and Nucleic Acids
Functional Diversity of Proteins u Catalysis: Enzymes: amylase, pepsin, lipase u Transport: hemoglobin, serum albumin u Nutrient and Storage: egg albumin,
PROTEINS. Protein Molecules Are very large and complex ( often called macromolecules) Made up of hydrogen, carbon, oxygen, nitrogen, and sometimes other.
7.4/14.1 PROTEINS. Protein’s have 4 levels of Structure: 1. Primary Structure = the order of amino acids that make up the polypeptide; amino acids are.
PROTEINS. Learning Outcomes: B4 - describe the chemical structure of proteins List functions of proteins Draw and describe the structure of an amino acid.
Proteins and amino acids
GENE EXPRESSION External Proteins  Are giant molecules (polymers) made out of amino acids (monomers).
Proteins Multipurpose molecules Proteins Most structurally & functionally diverse group of biomolecules Function: involved in almost everything.
By DC. H2OH2O How much of you is protein? Amino Acids: “Dry” form Carboxylic acid Amino group Radical group.
THE STRUCTURE AND FUNCTION OF MACROMOLECULES Proteins - Many Structures, Many Functions 1.A polypeptide is a polymer of amino acids connected to a specific.
Introduction to Proteins
Proteins… Let’s Review…… then….. Let’s discover proteins…. PollEv.com/tinalambiase209.
Molecules of Life Molecules of life are synthesized by living cells – Carbohydrates – Lipids – Proteins – Nucleic acids.
PROTEIN FUNCTIONS. PROTEIN FUNCTIONS (continued)
Amino Acids & Proteins The Molecules in Cells Ch 3.
Proteins: multipurpose molecules
PROTEINS L3 BIOLOGY. FACTS ABOUT PROTEINS: Contain the elements Carbon, Hydrogen, Oxygen, and NITROGEN Polymer is formed using 20 different amino acids.
L IPIDS © 2015 Pearson Education, Inc Fats are lipids that are mostly energy- storage molecules Lipids are water insoluble (hydrophobic, or water-
CHAPTER 5 THE STRUCTURE AND FUNCTION OF MACROMOLECULES Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings Section D: Proteins -
Proteins  Are the most diverse biomolecules. They make up muscles, skin, hair, enzymes, hormones, hemoglobin, and antibodies.  The basic structure unit.
Proteins. Protein (from the Greek protas meaning "of primary importance") is a complex, high-molecular-weight organic compound that consists of amino.
Qualitative Tests for Proteins
Chemistry: An Introduction to General, Organic, and Biological Chemistry, Eleventh Edition Copyright © 2012 by Pearson Education, Inc. Chapter 16 Amino.
Haemoglobin: Structure and Formation of Proteins 1.1.2, a, b,c.
Amino Acids, Proteins & Enzymes Chapter 16
Proteins What do we need proteins for?
PROTEINS and ENZYMES!.
Proteins Proteins make up more than 50% of the dry weight of cells
Protein Structure.
(4) Genes and proteins in health and disease
Proteins… Let’s Review…… then….. Let’s discover proteins….
Protein Structure Amino Acids Polypeptide Levels of Structure
Proteins.
Proteins 1 1.
Proteins Topic 7.5.
Multipurpose molecules
Macromolecules Part 2 Unit 1 Chapter 5.
See Page 563 Essential amino acids must be obtained from the diet.
Proteins Topic 7.5.
PROTEINS and ENZYMES!.
Chapter 19: Proteins.
Protein Structure Chapter 14.
Amino Acids.
Proteins.
Unit 7: Molecular Genetics 7.6 Proteins
Proteins.
Proteins.
Presentation transcript:

Importance, Characteristics, Structure, Classification, Denaturation

 Major structural components of animal tissues  Involved in the maintenance of life processes as communication (nerves), defense (antibodies), metabolic regulation (hormones), biochemical catalysis (enzymes), and oxygen transport (hemoglobin)  Utilized in the building of new tissues and maintaining tissues which are already developed

 Unlike fats and carbohydrates, proteins are not stored to any appreciable extent  They are giant polymers whose MW ranges from several thousands to millions  The elementary composition of most proteins are 55% C; 7% H; 23% O; 16% N; 1% S; and less than 1% P

 Primary – defined by the number, sequence and kind of amino acid linked by peptide bond  Secondary – any ordering of otherwise flexible peptide chain resulting from the formation of H- bonds between the carbonyl oxygen and the amide nitrogen of the polypeptide backbone  Tertiary – superfolding of the protein due to interactions between the different Rs of the amino acid  Quaternary – intermediate interactions between protein molecules which are folded and refolded can yield aggregates of individual molecules.

 According to Shape - Globular – more or less spherical to oblate or egg-shaped (Ex. Insulin, myoglobin) - fibrous – individual strands or bundles of lateral strands, elongated molecules highly resistant to digestion by proteolytic enzymes (Ex. Elastin and collagen, keratins, myosin, fibrin

 According to Function - Structural (collagen) - contractile proteins (myosin and actin) - antibodies (gamma globulins) - oxygen binding proteins – blood proteins or transport proteins - hormones - enzymes - nutrient protein

 Denaturation – unfolding of the complex secondary, tertiary and quaternary structure of proteins

 Heat – causes the atoms within the protein molecule to vibrate more rapidly, causing the hydrogen bonds and hydrophobic interactions to break  Strong acids – split salt linkages by ionizing the carboxylic group  Alcohol – disrupts the hydrogen bonds  Heavy metals (Ag, Pb and Hg) – combines the free carboxylate anions of the acidic amino acid with the metal, causing precipitation

 Organic acids (picric and tannic acids) – used to precipitate the alkaloids giving rise to the name alkaloidal reagents. The anion of the acid will react with the protonated amino groups of proteins, causing disruption of the salt linkages