can be done by protein electrophoresis. Protein electrophoresis involves the movement of proteins within an electric field with mobility being dependent on factors such as the size and shape (secondary and tertiary structure)‚ as well as the charge of the protein (due to primary structure). Other factors that can affect the mobility are electric-field strength‚ matrix pH‚ and ionic buffer strength of the electric field. Because there are so many factors involved in analyzing proteins during electrophoresis
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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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Expressing and Purifying the Recombinant form of Green Fluorescent Protein (rGFP) from the E.coli strain using Ni2+ agarose affinity chromatography technology Abstract The purpose of this experiment was to express and purify the his6-tagged recombinant form of GFP (rGFP) from the organism E.coli using Ni2+ agarose affinity chromatography. The expression of rGFP was confirmed qualitatively using the UV light and was expressed in the E.coli strain BL21 (DE3) (-- removed HTML --) (-- removed HTML
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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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Module 2 Section 2 EXPERIMENT: DNA & Protein Synthesis Exercise 1 – Modeling DNA 1. List the four bases which are found in DNA. (1 pt) The four bases found in DNA are cytosine‚ adenine‚ guanine and thymine. 2. Fit any six nucleotides together to form a row‚ then list the six nucleotides in the order you used them. Work with your model pieces and try fitting the bases together to make a double strand as shown in Figure 9 of the lab manual. Which nucleotides form pairs
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In order to purify CelB2 protein bound to maltose-binding-protein‚ amylose affinity chromatography was performed. The amylose resin present in 20% ethanol was first diluted by adding 10 mL of 20 mM TrisHCl‚ pH 7.4‚ 0.2 M NaCl‚ 1 mM EDTA and centrifuged at 700 rpm for 5 minutes. After decanting the buffer‚ another 10 mL of TrisHCl‚ pH 7.4‚ 0.2 M NaCl‚ 1 mM EDTA was added to this resin solution and centrifuged at 700 rpm for another 5 minutes to further dilute the ethanol concentration in the resin
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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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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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Structures‚ Biosynthesis and Biofunctions of Iron-sulfer proteins Yiming Chen‚ Brown University‚ May 11th‚ 2011 I. Introduction Iron-sulfur proteins are the proteins which contain iron-sulfur clusters‚ like sulfide-linked di-‚ tri-‚ and tetrairon centers with various oxidative states 1. An excess of 120 distinct types of enzymes and proteins are known to contain Fe-S clusters2. Iron-sulfur proteins are known for the role of the oxidation-reduction reactions of mitochondrial electron transportation
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Abstract The objective of this lab was to measure the amount of protein from a piece of beef liver . This was done by taking the liver‚ blending it and then using a centrifuge to separate the supernatant from the pellet. Once that was completed‚ ammonium sulfate was added to the supernatant‚ chilled and then spun for a second time. Next‚ 20 mL of water is added to the pellet‚ stirred and the volume was recorded. The teacher calculated the total mass of liver to be 10.098g. Lastly a spectronic
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