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study guide for principles of biochemistry mississippi state university
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O,C,H,N,P,S- most important elements for life Purines-2 rings, Adenine + Guanine Pyramidines-1 ring, Cytosine + Thymine Catabolism – breakdown of nutrients, produces ATP Anabolism – synthesis of larger macromolecules, consumes ATP Water can form up to 4 H-bonds Water is universal solvent, useful for temperature regulation and transportation of nutrients/waste in the body Dissolves polar substances by attracting the charged areas, forms solvation spheres Polar groups: Hydroxyl --OH Sulfhydryl --SH Amino –NH 2 Carbonyl Aledhyde –C- -OH Ketone –C- -O Carboxyl –COO- Charged groups Amino –NH 3 + Carboxyl –COO- Phosphoryl PO 4 2- Amphiphilic molecules (polar + nonpolar groups) form micelles in water (polar groups outward nonpolar inside) Ka= [H 3 O+][A-] // [HA] pH= pKa + log [A-]/[HA] Buffers resist pH change when acid or base is added (weak acid/conjugate base)
Amino Acid structure: Central carbon bonded to : Carboxyl group (COO-), Amino group (NH2), Hydrogen atom, R side chain (variation here) Amino acids in proteins are exclusively L stereoisomers Negative amino acids (Dicarboxylic) (Acidic) Aspartate ( CH2-COO-) Glutamate (CH2-CH2-COO-) Positive amino acids (Basic) Lysine Arginine Histidine Cysteine side chains Sulfur S cross link, form disulfide bridge Helps stabilize 3d tertiary protein structure Isoelectric point: pH value where net charge on molecule is 0 Ionization state of amino acids altered by change in pH pH > pI = negative charge pH< pI = positive charge For A.As with charged side chains: pI = [pKa of side chain + pka of amino acid group with same charge (COO- or NH3+)]/ Non charged side chains: pI = [pKa of COO- + pKa of NH3+]/ Peptide bond – Loss of OH from Carboxyl + H from amino, links amino acids, dehydration (loses water molecule) Peptide- Chain of <50 amino acids Polypeptide- Chain of >50 amino acids Protein – 1 or more polypeptides Protein structure Primary – amino acid sequence Secondary – repeated peptide chains (alpha helicies, beta sheets)
Control activity of existing enzymes – allosteric regulation (allosteric effectors bind to allosteric site, conformational changes, can improve or worsen enzyme activity) Most allosteric enzymes are multi subunit proteins Covalent modification ex. Phosphorylation – addition of phosphate group to a protein (serine, threonine, tyrosine) by protein kinase, can improve or worsen enzyme activity Sigmoidal curve