AFFINITY CHROMATOGRAPHY J.pptx
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Agarose Gel Electrophoresis Estimate the size of molecules Agarose in AGE Gel Loading Buffer Nucleic Acid Stain Factor affecting mobility of DNA Factor affecting Resolution Smearing
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Gel electrophoresis
Gel electrophoresis is a method to separate biomolecules like proteins, nucleic acids, and lipids based on their charge and size. During gel electrophoresis, an electric current is applied across a gel, causing negatively charged molecules to migrate toward the positive electrode and positively charged molecules to migrate toward the negative electrode. Smaller molecules migrate faster through the gel than larger molecules. Factors like the charge, size, and shape of molecules, as well as the electric current, gel composition, and buffer used, determine how far each type of molecule will migrate through the gel. Gel electrophoresis has applications in separating DNA, RNA, proteins, and other biomolecules.
AFFINITY CHROMATOGRAPHY
Affinity chromatography is a method used to separate biochemical mixtures based on highly specific interactions like antigen-antibody binding. It works by coupling a ligand to a stationary phase gel that can trap molecules of interest from a mobile phase solution. Unbound molecules are washed away while bound molecules are later released through elution. Common uses include purifying proteins, nucleic acids, antibodies, and enzymes from mixtures by exploiting properties like metal ion binding or interactions with lectins or ligands.
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Affinity chromatography
1.HISTORY OF AFFINITY CHROMATOGRAPHY
2.PRINCIPLE
3.TYPES
Lectin Affinity Chromatography
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4.APPLICATIONS
PAPER ELECTROPHORESIS.
In this slide contains types, working principle, factors affecting, advantage and disadvantage of paper electrophoresis.
Presented by: G.Sai Swetha. (Department of pharmacology),
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This document discusses protein motifs and domains. It defines a motif as a recurring arrangement of secondary structure found in multiple proteins, such as the HTH, HLH, and hairpin motifs. A domain contains one or more well-characterized motifs and has an independent function. Two common motifs are described: the HTH motif, which contains two antiparallel alpha helices connected by a beta turn for DNA binding; and the HLH motif, which contains two helices connected by a loop, with the larger helix binding DNA and the smaller helix aiding folding. Domains are defined as distinct functional units that are evolutionarily conserved and can exist independently; they are classified based on secondary structure composition.
Gas chromatography
Gas chromatography (GC) is a technique used to separate volatile organic compounds. It consists of a carrier gas, an injection port, a separation column, an oven, and a detector. Samples are vaporized and injected into the column where components separate based on interactions with the stationary phase. Separated components exit the column and are detected, producing a chromatogram. Common applications of GC include environmental monitoring, refinery and chemical plant process control, and analysis of biological samples.
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AFFINITY CHROMATOGRAPHY
Affinity chromatography is a method used to separate biochemical mixtures based on highly specific interactions like antigen-antibody binding. It works by coupling a ligand to a stationary phase gel that can trap molecules of interest from a mobile phase solution. Unbound molecules are washed away while bound molecules are later released through elution. Common uses include purifying proteins, nucleic acids, antibodies, and enzymes from mixtures by exploiting properties like metal ion binding or interactions with lectins or ligands.
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Affinity chromatography
1.HISTORY OF AFFINITY CHROMATOGRAPHY
2.PRINCIPLE
3.TYPES
Lectin Affinity Chromatography
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Metal Chelate Chromatography
Dye Ligand Chromatography
Covalent chromatography
4.APPLICATIONS
PAPER ELECTROPHORESIS.
In this slide contains types, working principle, factors affecting, advantage and disadvantage of paper electrophoresis.
Presented by: G.Sai Swetha. (Department of pharmacology),
RIPER, anantapur.
Protein structure determination
This document discusses various techniques for determining the primary, secondary, tertiary, and quaternary structures of proteins. It describes methods such as determining amino acid composition, degradation of proteins into smaller fragments, sequencing techniques like Edman degradation, and use of X-ray crystallography and NMR to analyze secondary and tertiary structures. Chromatography, electrophoresis, and centrifugation techniques are also covered for protein purification and separation.
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This document discusses protein motifs and domains. It defines a motif as a recurring arrangement of secondary structure found in multiple proteins, such as the HTH, HLH, and hairpin motifs. A domain contains one or more well-characterized motifs and has an independent function. Two common motifs are described: the HTH motif, which contains two antiparallel alpha helices connected by a beta turn for DNA binding; and the HLH motif, which contains two helices connected by a loop, with the larger helix binding DNA and the smaller helix aiding folding. Domains are defined as distinct functional units that are evolutionarily conserved and can exist independently; they are classified based on secondary structure composition.
Gas chromatography
Gas chromatography (GC) is a technique used to separate volatile organic compounds. It consists of a carrier gas, an injection port, a separation column, an oven, and a detector. Samples are vaporized and injected into the column where components separate based on interactions with the stationary phase. Separated components exit the column and are detected, producing a chromatogram. Common applications of GC include environmental monitoring, refinery and chemical plant process control, and analysis of biological samples.
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Paper electrophoresis
The technique of paper electrophoresis is simple and inexpensive and requires only micro quantities of plasma for separation.
The support medium is a filter paper
The electrophoresis apparatus in its simplest form consists of two troughs to contain buffer solution, through which electric current is passed.
Frequently used in isolating proteins, amino acids and oligopeptides.
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2.NUCLEAR MAGNETIC RESONANCE
PROTEIN STRUCTURE DETERMINATION
3. MASS SPECTROMETER
MALDI
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APPLICATIONS
CONCLUSION
REFERENCES
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In this slide contains introduction, methods, supporting media for zone electrophoresis.
Presented by: Mary Vishali. (Department of pharmacology),
RIPER, anantapur.
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INTRODUCTION
STRUCTURAL PROTEOMICS
WHAT IS THE IMPORTANCE OF STUDY OF PROTEIN
METHODS FOR SOLVING PROTEIN STRUCTURE
1. X- RAY CRYSTALLOGRAPHY
INTRODUCTION
PROCEDURE
LIMITATIONS
2.NUCLEAR MAGNETIC RESONANCE
PROTEIN STRUCTURE DETERMINATION
3. MASS SPECTROMETER
MALDI
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STRUCTURE MODELING
APPLICATIONS
CONCLUSION
REFERENCES
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Affinity chromatography is a powerful technique for purifying proteins using biological interactions like enzyme-substrate binding. It works by attaching a ligand with specific binding affinity to a stationary phase within a column. When a protein mixture is passed through, only the desired proteins that bind to the ligand will be retained while others pass through. Various methods can then be used to separate the purified proteins from the ligand, such as changing pH, salt concentration, or adding competitors. Affinity chromatography is useful for purifying molecules like antibodies, enzymes, and nucleic acids.
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1. Protein-ligand interaction refers to the binding of a small molecule ligand to a larger protein and is fundamental to many biological processes like enzyme catalysis and signal transduction.
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Affinity Chromatography.pptx
1. Affinity chromatography is a type of liquid chromatography that separates components based on a biological interaction between a ligand attached to a support and the target molecule in a sample.
2. The key components of affinity chromatography are the supporting matrix, ligand, and eluent. The ligand is attached to the supporting matrix and specifically binds the desired target molecule from a sample.
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Affinity Chromatography.pptx
Affinity chromatography is a method used to separate biomolecules from a mixture based on specific interactions between the molecules and a ligand attached to a chromatography matrix. It was developed in the 1930s and relies on reversible interactions like enzyme-substrate or antibody-antigen binding. The target molecule binds to the ligand while unbound molecules are washed away. Then, conditions are altered to dissociate the bound molecule from the ligand, eluting it from the column in a purified form. Affinity chromatography is widely used to purify proteins, nucleic acids, and other biomolecules.
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CELL MEMBRANE , RECEPTOR , DRUG RECEPTOR INTERACTION
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Affinity Chromoatograpy
Affinity chromatography is a technique that exploits specific biological interactions to purify biomolecules. It was first developed in the 1930s and relies on the reversible binding between a ligand coupled to a matrix and the target molecule from a sample. Recent advances enable exploration of protein interactions and modifications. Coupling affinity chromatography with mass spectrometry aids in biomarker discovery. The technique separates molecules based on their differential affinity for ligands, with unbound molecules washing away and bound molecules then eluted.
Aug 26 2011
The document discusses several key topics regarding proteins and enzymes:
1. It describes the primary structure of proteins and how their amino acid sequence determines their function. It also discusses polymorphic proteins and early protein sequencing methods.
2. Protein folding and the factors that influence a protein's three-dimensional structure are summarized, including non-covalent bonds, domains, and common structural motifs like alpha helices and beta sheets.
3. The roles of different protein types like globular, fibrous, and assembly proteins are highlighted. Key fibrous proteins like collagen and elastin are also mentioned.
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CELL MEMBRANE , RECEPTOR , DRUG RECEPTOR INTERACTION
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AFFINITY CHROMATOGRAPHY J.pptx
- 1. PRESENTED BY: PRASHANT V C DEPT OF ZOOLOGY GUK
- 2. First developed by Pedro Cuatrecasas and Meir Wilcheck in 1968. Used to study enzymes and other proteins. Relies on affinity of various biochemical molecules with specificity.
- 3. A method of seperating mixtures based on highly specific interations/affinity between the an immobilised ligand and target molecule. Ex. Antibody/antigen, enzyme/substrate, and enzyme/inhibitor interactions.
- 4. Based on 3 aspects : 1. Matrix : for ligand attachment. 2. Spacer arms : create space between ligand and matrix. If they are close to each other, then due to steric hindrance, the target molecules won’t be able to bind to the ligand. 3. Ligands : which has an affinity for target molecule. (reversible)
- 5. Provides attachment to affinity ligands. Amino , hydroxyl , carbonyl, etc. groups serve as ligand binding sites. Should be stable enough in various conditions like pH, salt concentrations etc. Should be porous ( surface area). Made of agarose, polyacrylamide, cellulose, silica etc.
- 6. Selection of ligand influenced by 2 factors: I. Ligand must exhibit specific and reversible binding affinity for target. II. Must have chemically modifiable groups that allow it to attach to matrix. • Ligands are attached to matrix by covalent bonds using functional groups located in matrix such as: Amine Carbonyl hydroxyl
- 7. Commonly used ligands Affinity Concanavalin A (lectin) Sugars, glycoproteins Wheat germ agglutinin (lectin) N-acetylglucosamine Avidin (protein) Biotin containing enzymes Proteins A and G Immunoglobulin IgG Poly (A) RNA containing poly (U) sequences Antibody (Immuno Affinity Chromatography) Antigen Histones DNA Acriflavin (antiseptic) Nucleotides Lysine rRNA Metal ions (Cu+2 , Ni+2 , Zn+2) (IMAC- Immobilised Metal ion Affinity Chromatography) Histidine containing proteins Hormone Receptor/ binding protein
- 8. Sample injected into column. Wash buffer – non target molecules elute off. Ligand/target complex will remain in column after wash buffer elutes off non target molecules. Elution buffer – disrupts interaction between target molecules and stationary phase/ligand. so target molecules are obtained.
- 10. Extremely high specificity. High degrees of purity can be obtained. Reduce the amount of substance in a mixture. Used in Genetic Engineering- Nucleic acid purification. Antibody purification from blood serum. To observe which biological compound bind to a particular substance.
- 11. Expensive ligands Leakage of ligands Degradation of solid support Non specific adsorption
- 12. https://en.wikipedia.org/wiki/Affinity_chromatography https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5206469/ Pictures available at: • https://www.shodex.com/en/da1/09/0201.html https://www.quora.com/What-is-affinity-chromatography https://www.slideshare.net/rajpalchoudharyjat/affinity- chromatography