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1 Evolutionary conservation and emerging functional diversity of the
1 Evolutionary conservation and emerging functional diversity of the

The significance of biochemical and molecular sample integrity in
The significance of biochemical and molecular sample integrity in

... state and the rapidity of death, may play major roles in determining the postmortem condition of the sample [6–9]. It would therefore be of importance to determine the condition and quality of postmortem tissue, for example, through the quantification of a biological marker in such sample. In a prev ...
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... G-Alpha is in a GDP bound state. When it interacts with the activated receptors, it undergoes its own conformational change, kicking out GDP from the binding site o Activated receptor acts as a Guanine Exchange Factor This allows GTP to interact with G-Alpha. When GTP binds, the G-Protein falls apar ...
Codon - Cloudfront.net
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... DNA and Translation • Gene: section of DNA that creates a specific protein – Approx 25,000 human genes • Proteins are used to build cells and tissue • Protein synthesis involves two processes: 1) Transcription 2) Translation ...
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Identification of a Fluorescent Protein from Rhacostoma Atlantica
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... to the Solute Carrier Family 1, along with human glutamate transporters (Excitatory Amino Acid Transporters EAATs). Neutral amino acid exchange via ASCT1 is thought to be coupled to only one Na+ ion. This is in contrast to the EAATs where glutamate transport is coupled to three Na+, one H+ ion and t ...
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MSc in Biochemistry Dissertation Project – 2nd Cycle Student´s

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... group” (2). The RDA for protein, which is based primarily on nitrogen balance studies, is 0.8 g/kg body weight per day for adults aged 19 y and is established from the EAR for protein (0.66 g/kg body weight per day) plus a safety variance of .20%. The EAR is defined as “the average daily nutrient in ...
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... as oxygen-carrying hemoglobin in red blood cells. 4. Defensive proteins such as the antibodies that provide protection against foreign substances that enter the bodies of animals. 5. Enzymes that regulate the rate of chemical reactions. Although the functions of proteins are diverse, their structure ...
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... molecules are forced into compact conformations that minimize their surface exposure to water. Note: hydrophobic bonding is not a kind of interaction between specific atoms in the hydrophobic part of a molecule. Rather, the hydrophobic part of the molecule conforms to the conformation imposed by the ...
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Biological Molecules Review Questions 2015

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... C. Transketolase and transaldolase link this pathway to gluconeogenesis. F D. It is more active in muscle cells than in fat-storage cells. F E. It interconverts trioses, tetroses, pentoses, hexoses, and heptoses. T 7. Which of the following statements are correct? The citric acid cycle (2 points) A. ...
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ADVANTAGES OF PORCINE BLOOD PLASMA AS A COMPONENT

- Universiti Malaysia Kelantan
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... because they hydrolyze peptide bonds in aqueous environments and synthesize peptide bonds in microaqueous environments (Ogino et al., 1999). Microbial proteases dominate the commercial applications, with a large market share taken by subtilisin proteases from Bacillus spp. for laundry detergent appl ...
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Überschrift – Thema, Arial 80 pt fett schwarz oder KIT-Grün

... The reason for the recalcitrance of these biofilms are so-called persister cells. Persisters are dormant variants of regular cells that form stochastically in microbial populations and are highly tolerant against modern antibiotics [1]. It is known that one protein plays a major role in persister ce ...
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BIOCHEMISTRY NATIONAL BOARD EXAM REVIEW

... 54. Polyuridylic acid in a cell-free system capable of protein synthesis results in production of polyphenylalanine. In this system, polyuridylic acid functions as A. B. C. D. E. ...
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Proteolysis



Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.
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