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moluceular lab 1
moluceular lab 1

... 1-H-bond : ( Binding between parts of near region and far region from poly-peptide ) 2-Ionic bond : (Binding between free of Amine group at one side of the poly-peptide with free of Carboxyl group on the other side of the poly-peptide 3-di-sulfide bond (-S-S-) :(Binding between two atom of sulfide i ...
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Fishy Genetics: From DNA to Protein: The Central Dogma of Biology

... DNA​  is  a  very  complex  molecule.    It  stores  the  information  for  making  proteins  in  the  codes  of  its  bases:  A,T,C,   &  G.    ​Proteins​  are  long  chain  molecules  (polymers)  that  are  made  of  ​amino  acids​  (monomers).    There  are  20   different  amino  acids.    Prote ...
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... Oxygen has been reduced (gained H’s). Oxygen was the oxidizing agent (acceptor of the H’s). ...
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... Protein shape is stabilized by: Weak interactions such as hydrogen bonding between side chains, ionic bonds between charged side chains, and hydrophobic interactions between nonpolar side chains Covalent linkages such as disulfide bridges between two cysteine monomers brought together by protein fol ...
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... • A collective name for the proteins expressed by the genome • Dynamic and functional information • It varies with cell type, developmental stage, and environmental condition such as the presence of hormones. • Regulation of mRNA synthesis, alternative splicing, mRNA stability, rate of protein synth ...
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Biology Unit 2
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... Carbon atoms or atoms of other elements. Carbon can also form multiple bonds (i.e. double and triple) with Carbon or atoms of other elements. Multiple bonds increase the “bonding strength”. III. Carbon and Hydrogen (called Hydrocarbons), when bonded, provide the “backbones” that make up many organic ...
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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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