of a functional recombinant fusion protein via the directional sub-cloning of an E.coli derived tyrosine phosphatase gene (wzb) into a pT5(6H)CFP mutant expression vector. Abstract: Application of fluorescent fusion proteins to the field of expression and interaction proteomics as a means of dynamic imaging proteins in vivo has allowed for rapid advancements in biotechnology research. Production of such proteins first involves the insertion of a given protein-coding gene transcriptionally in-frame
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Task 1 • Describe the structure of an enzyme as a protein‚ in terms of tertiary/ quaternary structures. 1) Primary Structure This is in reference to the order of way that amino acids are connected to form a protein. These are built up from 20 amino acids‚ and follow these structures o A carbon (the alpha carbon) bonded to the four groups below: o A hydrogen atom (H) o A Carboxyl group (-COOH) o An Amino group (-NH2) o A "variable" group or "R" group 2) Secondary Structure This is in reference
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Na’imat. Reg. No. : 0105514. Course: Immunology laboratory. Instructor: Dr. Muna Hassuneh. Report subject: Serum protein electrophoresis. Report No.: 1. Serum Protein Electrophoresis (SPEP) Introduction: The serum protein electrophoresis (SPEP) test measures specific proteins in the blood to help identify some diseases. And its uses an electrical field to separate the proteins in the blood serum into groups of similar size‚ shape‚ and charge. And here we’ll use gel electrophoresis which
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Separation of Proteins and Mass Analysis Using SDS PAGE Biology 00-01L Abstract This experiment consisted of separating proteins into polypeptides using a method called SDS PAGE which is a type of electrophoresis. The polypeptides had different masses‚ so each polypeptide traveled a different distance and this was an essential part of the lab which demonstrated that there exists a relationship between the distance traveled by the protein and the mass of the protein. This relationship was graphed
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PROTEIN ARTICLE RESEARCH SCI/241 PROTEIN ARTICLE RESEARCH Proteins are a part of every cell‚ tissue‚ and organ in our bodies. The protein we eat is broken down by amino acids that are later used to replace proteins in our bodies. These proteins include meats‚ poultry‚ fish‚ eggs‚ nuts‚ seeds‚ milk and milk products. Proteins are made up of amino acids. There are 20 different amino acids that join together to make up all types of protein. A complete protein source is one that provides all
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CHARACTERIZATION OF PROTEINS Abstract Different techniques and principles for protein extraction and characterization were demonstrated in this experiment. Various proteins were extracted from different sources: 1.67 g yeast invertase‚ 1.03 g egg white albumin‚ and 5.15 g of milk casein. Activity assay for invertase was performed using Benedict’s test and the enzymes inverting action on sucrose was confirmed. Warburg-Christian Method and Bradford Assay were also employed to determine the protein concentration
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Protein in the Digestive System Taylor Adams Biol 112- 501 18 April 2016 Introduction Proteins are found in nearly all foods that we eat. Once the food we eat makes its way to our stomachs‚ pepsinogen is released from chief cells. This enzyme mixes with hydrochloric acid in the stomach and begins to break down the proteins. Along with the stomach‚ the small intestine is also an important location for protein breakdown. The proteins from both locations are broken down into amino
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Protein and Amino Acid Supplementation in Sports The popularity of increasing the “performance-enhancing” supplements‚ Protein and amino acids‚ has flourished among all athletes. This increase is attributed to the belief by many of the athletes that it provides endurance‚ strength and speed enhancement. Amino Acids (AA) enhanced physical feats‚ improved energy and recovery sooner from fatigue. The three vital Amino Acids which were given a high focal point among athletes are leucine‚ isoleucine
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THE ROLE OF PROTEIN MISFOLDING AND AGGREGATION IN BSE When a protein misfolds it changes its behavior and function. If it becomes hydrophobic after once being polar. The properties and functionality of the protein are no longer useful to the organism and disaster results. PrPSc is hydrophobic‚ it avoids water inside of the cell…it attracts and attaches other proteins to misfolds and become hydrophobic …Misfolding spreads because the PrPSc act as chaperone proteins to convert PrPc TO PrPSc and
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Specificity of Protein-Ligand Binding 1). One can conclude that Orange G. has the lowest affinity for the albumin. In the experiment the concentration of Orange G that binds to protein was a lot less than either Ponceau S. or Bromophenol blue. The ligand with the highest affinity to BSA was a little more difficult to decipher. The experiment shows that all of the 2 µL of both Ponceau S. and Bromophenol blue bind to the BSA. However‚ when 5 µL of the ligand is added the BSA is saturated and cannot
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