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University of Lincoln RIF Studentships 2014 PROJECT DETAILS
University of Lincoln RIF Studentships 2014 PROJECT DETAILS

... Society is currently facing a worldwide pandemic of multidrug resistance bacteria, arising from the long-term use of antibiotics. In a clinical setting these strains proliferate under antibacterial treatment, resulting in sepsis and often life-threatening levels of infection. As part of the measures ...
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... sometimes covalent bonds). Polar residues are often found in active sites, to create a specific electrostatic environment within the cleft that forms the active site. Apparent pKa values for side chains of amino acids within proteins are often different from those for free amino acids. ...


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secret codon
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... in the chain is determined by the DNA sequence of the gene that encodes for it. DNA is a long chain of four different nucleotides (adenine, thymine, cytosine, and guanine), often abbreviated A, G, C, and T. These 4 nucleotides (sometimes referred to as bases) need to give instructions for the 20 dif ...
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... Protein of unknown function, copurifies with late Golgi vesicles containing the v-SNARE Tlg2p Lipid-binding protein containing three calcium and lipid binding domains; non-tagged protein localizes to mitochondria and GFP-fusion protein localizes to the cell periphery; C-termini of Tcb1p, Tcb2p and T ...
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... from date of despatch. Aliquots of stock solution can be kept frozen at -20°C for two years from date of reconstitution; do not freeze working dilutions. optimal dilution should be tested by serial dilution. 5g/ml (1:50) Formalin / Paraffin (pretreatment with microwave required, see protocol under ...
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... POTEETE1980) has proven to be a rich model system in which to study protein structure/function relationships at the protein sequence level. Each monomer in the mature tailspike trimer contains 666 amino acids after removal of its N-terminal Met residue (SAUERet al. 1982). The mature wild type trimer ...
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REVIEWS How membrane proteins travel across the mitochondrial

... Both models raise intriguing questions. What is the mechanism by which the precursor is handed from one complex to another? Do the two 70 kDa complexes select the imported substrates as they emerge from the TOM complex? Is the transfer of the precursor between the different Tim proteins mediated by ...
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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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