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lecture15
lecture15

... Wimley and White Hydrophobicity Measurements 3 papers: ...
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... • Glucose is the primary source of energy. • Glucose can be stored as glycogen, and converted to and stored as fat. • Glucose can be catabolized anaerobically and aerobically. Anaerobically, glucose is incompletely broken down (glycolysis) into lactic acid and small amounts of ATP. Aerobically, gluc ...
Chemistry Review
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... 3. Tertiary Structure – occurs when the secondary structure folds up in a very specific shape and forms a specific protein. The tertiary structure comes from interactions/bonds between the R groups of the amino acid. Some of the interactions that occur between amino acid R groups are: ...
Poster - Protein Information Resource
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Product: Cat. No.: Lot No.: Synonyms: Size: Storage: Usage: Product

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... Three-dimensional structure reveals the layouts of functional groups and amino acid residues of proteins. This means that the structural basis for a specific reaction to occur is clarified. However, the resolution of 10 pm is not sufficient to unveil the black box. In order to unveil the black box, ...
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influence of macromolecular crowding on protein stability
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... its biological function, a protein much fold into a single, well defined conformational state: the native state. Protein folding is thus the physico-chemical process by which a polypeptidic chain undergoes a structural change from an ensemble of coil like structure up to the unique structure encoded ...
DNA`s Discovery and Structure
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... The DNA has a triplet code using only the 4 nucleotides, A,C,G and T. Only 3 nucleotides form a triplet which, when in a gene, codes for a part of a protein. There are 34 total different triplets that can be created but only 20 different amino acids. (Would a doublet code work just as well?? i.e. on ...
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Protein Structure-Function Relationships - IBIVU

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Protein adsorption



Adsorption (not to be mistaken for absorption) is the accumulation and adhesion of molecules, atoms, ions, or larger particles to a surface, but without surface penetration occurring. The adsorption of larger biomolecules such as proteins is of high physiological relevance, and as such they adsorb with different mechanisms than their molecular or atomic analogs. Some of the major driving forces behind protein adsorption include: surface energy, intermolecular forces, hydrophobicity, and ionic or electrostatic interaction. By knowing how these factors affect protein adsorption, they can then be manipulated by machining, alloying, and other engineering techniques to select for the most optimal performance in biomedical or physiological applications.
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