Proteins are made up of long chains of amino acids‚ just a chain of ami. tacids makes up the primary structure. The secondary structure is formed by hydrogen bonds joining the chains in certain places to make an alpha helix or a beta sheet. The tertiary structure is formed by even more folding and joining of the chains to make a globular mass or fibrous mass. An example of this would be a carrier protein. Proteins are needed for many things they are needed in our diet for growth and repair of cells
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Estimation of protein concentration Introduction Protein assays are designed to measure the total protein in a solution. Protein assays are quantitative if the protein to be assayed is available in sufficient quantity such that one is able to use it to create a standard curve. If this cannot be achieved‚ then a standard protein‚ such as albumin‚ may be used for a standard curve with the understanding that the results on the unknown protein are semi-quantitative. Since most proteins are not available
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Describe how Bacteria decode its genetic information to produce proteins? Intro(10mins) Bacteria belongs to a group of organism that lacks cell nucleus and membrane bound organells. This group of organisms are termed as prokaryotes. Prokaryotes follows the central dogma of molecular biology first proposed by Francis Crick in 1958 to synthesize proteins from mRNA through a process called translation and the mRNA is being synthesized from the DNA by another process called Transcription.
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Analysis of protein post-translational modifications using DIGE-based proteomics Robert M. DeKroon‚ Jennifer B. Robinette‚ Cristina Osorio‚ Sun Yong Jeong‚ Eric Hamlett‚ Mihaela Mocanu and Oscar Alzate Summary Difference gel electrophoresis (DIGE) is most often used to assess relative changes in the expression levels of individual proteins in multiple complex samples‚ and this information is valuable in making inferences about relative protein activity. However‚ a protein‟s activity is not
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really been a problem throughout the years. There was one case in 2012 but the meat was properly disposed of by the United States Department of Agriculture (USDA). Testing for the disease can be difficult because there are only small traces of prion protein in the blood or urine so the only reliable test comes from a necropsy. However‚ with newer technology‚ detecting the disease has come a little be easier because technology has become more developed and sensitive when it comes to detecting the disease
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Spongiform Encephalopathy: Prions -Prion:the improper folding of a protein in the brain named PrPc. 2 important properties: -It is an infectious protein (PrPSc) that destroys nerve cells in the amyloid plaques of the brain and can lead to loss of brain function or dementia. -Has the ability to make more copies of the same misfolded protein over and over again. (Ahern & Rajagopal‚2012) Bovine Spongiform Encephalopathy: Chaperone Protein -misfolding of PrPc -> PrPSc = BSE -PrPSc passes
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The Spectrophotometer Determination Of Protein Concentrations And The Effects Sodium Dodecyl Sulphate And Triton X-100 Have On Protein Concentration. INTRODUCTION Spectroscopy is used as a collective term for all the analytical techniques based on the interaction of light and matter. Spectrophotometry is one of the branches of spectroscopy where we measure the absorption of light by molecules that are in a gas or vapour state or dissolved molecules/ions (Tombs‚ et.al‚ 1959). Spectroscopy is the
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Diagram of Essential Amino Acid Lysine ● ● Lysine is a base Physical properties: Polar‚ positively charged ● ● ● Highly reactive Hydrophilic Solubility: ^ soluble in cold water ● ● Reactivity: 0 Flammability: 1 (may be combustible at high temps Protein Structure Dehydration Hydrolysis Stabilizing Forces 1) Hydrophobic Interactions Non polar amino acids (leucine and phenylalanine are two examples). Weakest type of bond. 2) Hydrogen bonds: Polar or charged amino acids (example Tyrosine).
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VIETNAM NATIONAL UNIVERSITY – HOCHIMINH CITY INTERNATIONAL UNIVERSITY School of Biotechnology EXPRESSION OF PROTEIN ANTIGEN HIV -1 P24 IN TRANSGENIC TOBACCO PLANTS A thesis submitted to The School of Biotechnology‚ International University In partial fulfillment of the requirements for the degree of B.S. in Biotechnology Student name: Nguyen Ngoc Tu Anh – BT050036 Supervisor: Dr. Nguyen Thi Thanh
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Fold This method of folding napkins is very simple and can be done with almost any napkin without a need for starch. It adds a flowing‚ elegant look to your table. 1. Lay the napkin face down in front of you. 2. Fold the napkin in half and orient the open end towards you. 3. Fold the far-right corner over to the center of the side that is closest to you. The edge of this fold should run down the center of the napkin. 4. Repeat the last step with the other side‚ folding the far-left corner
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