ILO 1-Explain the chemical structure,classification, and properties of amino acids and how peptides are formed. 2-Describe the order of protein organization.

Slides:

Advertisements

Similar presentations

(carbon-based compounds)

Advertisements

Definition: Proteins are organic compounds with a high molecular weight formed of carbon, oxygen, hydrogen and nitrogen and may also contain sulfur,

simple protein hydrolyze to yield only amino acids e.g.: albumins, globulins. conjugated protein is a protein that functions in interaction with other.

Biochemistry of Proteins: function and classification.

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.

Kulsoom Structure & Classification of Proteins Dr. Bibi Kulsoom 1.

Proteins. What are Proteins? The most complex biological molecules Contain C, H, O and N Sometimes contain S May form complexes with other molecules containing.

Biochemistry of Plant Cells: The plant body consists of a large number of chemical elements(C, H, O and N) and different organic constituents as follows:

CHE 242 Unit VIII The Structure, Properties, Reactions and Mechanisms of Carboxylic Acids and Their Derivatives CHAPTER TWENTY-FOUR Terrence P. Sherlock.

Introduction to Amino Acids of Medical Importance

Biochemical instrumental analysis-7 Dr. Maha Al-Sedik.

Proteins. Other than water, protein are the chief constituents of the cells of the body. Proteins are much more complex than carbohydrates or lipids.

1) Properties of Water Water is a polar covalent solvent

Isolation of casein from milk

Biochemistry I BIOCA2301. Topics Carbohydrates Lipids Proteins Nucleic acids Enzymes Metabolism Carbohydrates Lipids Proteins Nucleic acids Enzymes Metabolism.

Chapter 7: Analysis of specific proteins & protein quality

Topic 7.5 Proteins (AHL).

Structure of proteins Vladimíra Kvasnicová. Chemical nature of proteins biopolymers of amino acids macromolecules (M r > )

Dr. Tarek El Sewedy Department of Medical Laboratory Technology Faculty of Allied Medical Sciences Faculty of Allied Medical Sciences.

Classification of proteins: I- According to Shape: i- Fibrous proteins: - Polypeptide chains are folded into filaments or sheets (rod or thread-shaped.

PROTEINS C, H, O, N, (S) Polymers made from chains of amino acids 20 amino acids used Linked by a peptide bond.

Chemical Level of Organization Chapter 2 Atoms, Molecules and Bonds.

 Denaturation; It is a process that leads to the protein losing its native 3 dimensional confirmation to a random confirmation without affecting its.

Organic Compounds Emily and Lauren. Carbohydrates Carbohydrates have a 2:1 ratio of hydrogen to oxygen. Ex. Glucose C 6 H 12 O 6 When sugars are broken.

Biochemistry of Plant Cells:  Carbohydrates  Vitamins  Proteins  Lipids  Nucleic Acids  Enzymes and Co-enzymes.

Basic Chemistry. Biochemistry: Essentials for Life Organic compounds Organic compounds –Contain carbon –Most are covalently bonded –Example: C 6 H 12.

Biochemistry: Chemistry of Life

PowerPoint ® Lecture Slide Presentation by Patty Bostwick-Taylor, Florence-Darlington Technical College Copyright © 2009 Pearson Education, Inc., publishing.

Section 1: Atoms, Elements and Compounds.  Elements pure substances that cannot be broken down chemically  There are 4 main elements that make up 90%

Amino Acids & Proteins The Molecules in Cells Ch 3.

Organic Molecules and Water.   Carbon Organic chemistry involves the study of carbon-containing compounds associated with life.

ORGANIC CHEMISTRY Organic compounds always contain carbon and hydrogen. Inorganic compounds typically lack carbon.

ILO 1-Explain the chemical structure,classification, and properties of amino acids and how peptides are formed. 2-Describe the order of protein organization.

1 2 It Matters! 3 Energy 4 Chemical Bonds 5 Water properties.

Chapter 2 Chemistry of Life Section 1: Nature of Matter.

Option B Biochemistry Jeff Venables Northwestern High School.

Proteins consist of amino acids which are characterized by the - CH(NH2)COOH substructure. Nitrogen and two hydrogens comprise the amino group, -NH2, and.

Proteins  Are the most diverse biomolecules. They make up muscles, skin, hair, enzymes, hormones, hemoglobin, and antibodies.  The basic structure unit.

Objectives Describe the chemical composition and general structure of carbohydrates. Describe three classes of carbohydrates, how they are synthesized,

Peptides. Structure and functions of proteins Department of General Chemistry Poznań University of Medical Sciences MD 2015/16.

Protein chemistry Lecture Amino acids are the basic structural units of proteins consisting of: - Amino group, (-NH2) - Carboxyl group(-COOH)

Unit 4.A 1 – Biomolecules.

Isolation of casein from milk

CLASSIFICATION OF PROTEINS.

Each amino acid shares a common structure, with an amine group (NH2),

LECTURE PROTEINS - Complex organic substances present in all living matter (plants, animals and microorganisms). - ALL proteins, apart from consisting.

Isolation of casein from milk

Carbon Compounds Macromolecules.

Atoms are composed of: _______: negatively charged particles

CONJUGATED PROTEINS.

Unit 9: Organic Composition of Food

Qualitative tests of protein

The chemicals that make things living!

UNIT 9 CS THE CHEMISTRY OF PROTEINS

Chapter 2 Organic Compounds

Isolation of casein from milk

Biochemistry - Macromolecules

Determination of Serum Total Protein Concentration

INTRODCTION TO MACROMOLECULES.   A homogeneous non-crystalline substance consisting of large molecules or ultramicroscopic particles of one substance.

CLASSIFICATION OF PROTEINS.

Organic Chemistry Department of Biology, WCU.

Isolation of casein from milk

Proteins Biopolymers of amino acids

Presentation transcript:

ILO 1-Explain the chemical structure,classification, and properties of amino acids and how peptides are formed. 2-Describe the order of protein organization. 3-Relate the structures of amino acids and proteins to their properties. 4-Describe the physical and chemical changes due to protein denaturation 5-state different classifications of proteins giving examples. 6-Explain protein folding and pathophysiological consequences of protein misfolding. 1-Explain the chemical structure,classification, and properties of amino acids and how peptides are formed. 2-Describe the order of protein organization. 3-Relate the structures of amino acids and proteins to their properties. 4-Describe the physical and chemical changes due to protein denaturation 5-state different classifications of proteins giving examples. 6-Explain protein folding and pathophysiological consequences of protein misfolding.

Amino acid structure Amino acid properties Protein structure Forces that stabilize protein structure Levels of protein organization Protein Classification Protein folding Protein misfolding Denaturation Outlines

Protein classificatio n Protein properties

+ Protein Classification By :DR.Marwa Matboly

No Universal system for protein classification According to structureAccording to biological activitiesAccording to shape(axial ratio)According to solubility Protein classification

Classification according to structure Simple proteins Formed only of amino acids e.g. albumin, globulin Compound protein Proteins containing amino acids+ other group e.g. phosphoprotein, lipoprotein, Derived proteins Hydrolytic products Denaturation products

Simple proteins Albumin (serum albumin, lactalbumin, and ovalbumin) Some Globulins(serum globulins are glycoproteins not simple proteins)

Compound proteins Amino acids Other group (prosthetic) Compound=conjugated protein

Compound proteins Contain phosphate attached to serine or theronine residues f the protein. e.g. casein of milk Phosphoproteins They are proteins usually basic proteins (histones) combined to nucleic acids. DNA of chromosomes is negatively charged, combine with the positively charged basic protein e.g. histones. Nucleoproteins

Compound proteins Contain lipids e. g. plasma lipoproteins: LDL: low density lipoproteins HDL: high density lipoprotein Lipoproteins Contain a metal: e. g. Iron containing transferritin Copper containing ceruloplasmin Zinc containing carboxypeptidase Metalloproteins Contain a colored prosthetic grop:protoporphyrin Eg Hemogloin Chlorophyl protein hemocyanin Chromoproteins

Compound proteins Protein covalently linked to short branched carbohydrates Glycoproteins Protein covalently linked to large carbohydrates part. Proteoglycan =glycosaminoglycan

Derived proteins Hydrolytic products peptonespeptides Denaturatio n products Metaproteins Coagulated proteins

Classification according to biological value High biological value proteins Contain all essential amino acids required for synthesis of human tissue proteins. Proteins of animal origin: meat liver, milk, fish Some Plant Proteins(beans, lentils, potato) Low biological value proteins Lack one or more essential amino acids Most plant protein(zein of maize deficient in tryptophan and lysine) Non digestible scleroproteins; eg. Scleroproteins. Gelatin, produced by boiling of collagen

High biological value protein Low biological value protein

Classification according to shape Axial ratio>10 Fibrous protein Axial ratio<10 Globular proteins

Classification according to solubility Soluble in water; albumin Soluble in dilute salt solution; globulin Proteins soluble Scleroproteins which are fibrous proteins with structural and supportive functions, e.g. keratin Proteins insoluble in water or any neutral solvents

+ Properties of proteins

Most abundant macromolecules in living cells Formed of C, H, N Nitrogen contents of protein is 16% Most proteins contain about 1% sulphur.

Proteins are amphoteric weak acidic groups Weak basic R groups Free NH2 Free COOH They act as an acid or base

Cytosolic proteins for colloidal solution(size nm and have the same charge),and non dialyzable

 PI of protein=zwitter ion(dipolar ion) It is pH at which a protein carries net zero charge the protein is electrically neutral the protein will not migrate in electric field Protein will be precipitated

At pH <pI of the protein Protein is Positively charged. Protein migrate towards the cathode in electrophoresis. At pH >pI of the protein Protein is negatively charged Protein migrate towards the anode in electrophoresis.