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Nutrients - SBI3URHKing
Nutrients - SBI3URHKing

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Experimental phase diagrams to optimise membrane protein

... The PhD project is part of the EU Marie Skłodowska Curie Action (MSCA) network RAtionalising Membrane Protein crystallisation (RAMP). Other PhD students in the network will use multidisciplinary approaches, including structural biology, microfluidics, and coarse-grained modelling to better understan ...
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... Function: Provide structure for tissues and organs, allow muscles to contract, transport oxygen, and make up enzymes which carry out chemical reactions. ...
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Chemistry Comes Alive: Part B Classes of Compounds • Inorganic

... • pH change interferes with cell function and may damage living tissue • Slight change in pH can be fatal • pH is regulated by kidneys, lungs, and buffers Buffers • Mixture of compounds that resist pH changes • Convert strong (completely dissociated) acids or bases into weak (slightly dissociated) o ...
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... • Chemical properties and reactivity are a result of functional groups- a configuration of atoms attached to the carbon skeleton • Functional groups maintain chemical properties no matter where they occur • Polar molecules are hydrophilic • Nonpolar molecules are hydrophobic • The degree to which or ...
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7. Protein Function

... There are two classes of MHC proteins which differ in their distribution among cell types and in the source of digested proteins Class I MHC - are found on the surface of virtually all vertebrate cells. These complexes of peptides and class I MHC proteins are the recognition targets of the T-cell re ...
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Basic Chemistry and Biochemistry Unit Review Sheet File

PROTEINS (Polymers of Amino Acids)
PROTEINS (Polymers of Amino Acids)

... 20 Amino Acids • Grouped by properties of their side chains – Non-polar (hydrophobic) – Polar (hydrophilic) – Acidic (-COOH grp) – Basic (-NH2) ...
R–groups
R–groups

... e. disulfide bridges― covalent bonds between two cysteine amino acids with sulfhydryl groups are brought close enough together by the folding of the protein D. Quaternary Structure― when two or more polypeptide chains are joined together by bonds or interactions of their R–groups. Same as a–e above. ...
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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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