characterized by the expression of muscle-specific proteins. The results showed that that myosin light chain was not present. It was concluded that the cells were not differentiated enough to begin with‚ the amount of cells used was not sufficient and the differentiation media did not have a neutral pH at the time of harvest. Introduction The purpose of the experiment was to differentiate C2C12 cells into muscle cells and tests for presence of muscle protein specifics. The hypothesis was that proliferating
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Erythrocyte: Structure & Metabolism หัวข้อบรรยาย 1. Red cell membrane 1. Membrane lipid 2. Membrane skeleton 3. Peripheral proteins 4. Integral proteins 2. RBC metabolism 1. Glycolytic (Embden-Meyerhof) pathway 2. Hexose monophosphate shunt 3. Rapoport-Luebering pathway 2.4 Methemoglobin reductase pathwa 3. Hemoglobin 3.1 Hemoglobin structure 3.2 Hemoglobin synthesis
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purification process. The Ni2+-NTA-Agarose resin was effective for this experiment‚ but testing other resins can determine if the Ni2+-NTA-Agarose resin was the best resin to use in this purification process. It also needs to be determined if running the protein through the column would have any effect on the dialysis process. This information can be determined by running dialysis with the crude sample and comparing the fold purity to the post-dialysis elution pool. Another future experiment‚ would be to
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This arrangement prevents the transport of water in and out of the cell. The phospholipid bilayer also contains proteins (intrinsic) which acts as a carrier to transport water-soluble substances across the membrane. Some proteins such as carrier proteins are also embedded in the bilayer. When a molecule that is specific to the protein‚ it binds to the protein‚ which causes the carrier protein to change shape in a way that the molecule is released inside the membrane. This occurs in facilitated diffusion
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e incorporated a fusion tag prior to our genes of interest and attached the expressed fusion proteins covalently on microarrays. This enhances the specific binding of the proteins compared to nitrocellulose. Thus‚ it helps to reduce the number of false positives significantly. It enables us to screen for immunogenic proteins in a shorter The correct insert size was determined by Colony PCR. Plasmids from clones containing the correct-sized inserts were isolated and the MCS was sequenced using both
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• M protein: Streptococcus pyogenes • Form biofilms How bacterial pathogens penetrate host defense • • • • • • Capsules Cell wall components Enzymes Antigenic variation Penetration into the host cell cytoskeleton; invasin Intracellular growth Capsules • Prevent phagocytosis Streptococcus pneumoniae Haemophilus influenzae Bacillus anthracis Cell Wall Components • M protein resists phagocytosis and improves adherence Streptococcus pyogenes • Fimbriae & Opa protein attachment
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University of Wisconsin-Madison may have discovered a link between zinc deficiency and protein clumping‚ in an experiment using a yeast solution‚ suggesting that it may be potential factors for disease like Parkinson’s and Alzheimer’s‚ if duplicated in humans. Questions or Relationship Shape is vital to proteins. When the correct shape is formed and present‚ cells behave as they indispensable should. When proteins lose their shape‚ they clump together. Parkinson’s and Alzheimer’s share these clumping
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dependent and ρ- independent. ρ – Independent termination (also known as intrinsic termination) does not use ρ factor protein to carry out termination. Sequencing of the entire E. coli genome has shown that most operons have Rho-independent termination sites. A hairpin loop forms from a palindrome
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PROTEIN ENERGY MALNUTRION Types include:[2] * Kwashiorkor (protein malnutrition predominant) * Marasmus (deficiency in both calorie and protein nutrition) * Marasmic Kwashiorkor (marked protein deficiency and marked calorie insufficiency signs present‚ sometimes referred to as the most severe form of malnutrition) Note that this may also be secondary to other conditions such as chronic renal disease[3] or cancer cachexia[4] in which protein energy wasting may occur. Protein-energy
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Nehru University‚ New Delhi‚ India‚ 2 School of Information Technology‚ Jawaharlal Nehru University‚ New Delhi‚ India Abstract CaMdr1p is a multidrug MFS transporter of pathogenic Candida albicans. An over-expression of the gene encoding this protein is linked to clinically encountered azole resistance. In-depth knowledge of the structure and function of CaMdr1p is necessary for an effective design of modulators or inhibitors of this efflux transporter. Towards this goal‚ in this study‚ we have
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