Biochemistry Flashcards

5371851283	Carbs	-CHO 1-2-1 -monomer= glucose -polymer= groups of glucose -Bio examples= cell walls of plants: cellulose, chitin -Energy: 4cal/g, 1ST SOURCE	0
5371851349	Lipids	-CHO (lots of C's and H's, little O's) -Monomer= fatty acids/ glycerol -polymers= saturated and unsaturated fats -Bio examples= blubber, phospholipid bilayer -Energy: 9cal/g, 2ND SOURCE	1
5371853413	Proteins	-CHON -monomer= amino acids -polymer= polypeptides/ protein -Bio examples= hair, muscles, skin -Energy: 4cal/g, LAST SOURCE	2
5371853414	Nucleic Acids	-CHONP -monomer= nucleotides -polymer= DNA, RNA -Bio examples= DNA and RNA -Energy: not a source of energy	3
5371887843	Primary Structure	amino acids are joined together	4
5372105423	Primary interaction	Peptide bonds join together amino acids (C-N)	5
5371887844	Secondary Structure	3D shape -alpha helix -beta pleated shape	6
5372126888	Secondary interaction	H-bond between amine group of one amino acid and the carboxyl group of another- (Hydrogen to oxygen)	7
5371889522	Tertiary Structure	Complex globular shape due to R-group interactions	8
5372148887	Tertiary Interaction	-hydrophobic interactions -van der waals -disulfide bridges (cysteins are attracted to each other) -enzymes hold them together	9
5371889523	Quaternary Structure	Multiple tertiary structures put together	10
5372161775	Function of Enzymes	To lower the activation energy and start the reaction faster	11
5372222662	Structure of enzymes	-Enzymes have to be specific to its substrate in order to fit -Substrate bonds to enzyme's active site	12
5373454141	Normal vs. Allosteric	normal= one active site allosteric= more than one active sit	13
5373832546	catalyzed reaction		14
5373461433	Negative feedback	Inhibition stops a biochemical pathway from making product.	15
5373465286	Competitive Inhibition	-blocks the active site -competitor makes substrate unable to connect with active site	16
5373471816	Non-competitive Inhibitition	-Binds to allosteric site and causes a conformational change in active site, so substrate can no longer bind	17
5373483807	Environmental factors that influence enzyme activity	-temperature -pH -substrate concentration (increase substrate= no change in rxn rate) -enzyme concentration (increase enzyme= increase in rxn rate)	18
5373846652	Exergonic reaction	-reaction is spontaneous -products have less energy -energy is released	19
5373850744	Endergonic reaction	-reaction is not spontaneous -reactants have less energy -energy is absorbed	20
5373814908	Denaturing enzyme	permanently deforming enzyme -active site no longer the correct shape -acids/bases change the bonding of R-groups in the active site -heat= destroys and changes shape permanently -cold= molecular movements decrease, less substrate/enzyme interaction	21
5373584612	Hydroxyl	-OH -Polar -Hydrophilic -found in ALL Nucleic Acids	22
5373598165	Methal	-CH3 -non-polar -hydrophobic -found in many lipids	23
5373603719	Carboxyl	-COOH -polar -hydrophilic -acidic	24
5373607541	Carbonyl	-CO -polar -hydrophilic -acidic	25
5373622975	Amine	-NH2 -polar -hydrophilic -found in all proteins	26
5373658924	Sulfydryl	-SH -polar -hydrophilic -forms disulfide bridges in proteins	27
5373667817	Phosphate	-PO4 -polar -hydrophilic -phospholipids -ALL nucleic acids	28
5373680906	Dehydration synthesis	putting monomers together to make polymers -creates H20 -forms peptide bonds	29
5373706567	Properties of water	-Choesion -Adhesion -Solvent -High specific heat -high vaporization -Density- water is less dense when solid and most dense at 4 degrees C	30
5373786462	Acids	-pH of below 7 -excess of H+ ions	31
5373786463	Bases	-pH of above 7 -excess -OH ions	32
5373796196	Buffers	substances that minimize changes in pH. Accept H+ from solution when they're in excess and donate H+ when they're depleted. -more acidic= H+ ions increasing, moves to left of rxn -more basic= -OH ions increasing, moves to right of rxn	33