EK Ch 1: Biological Molecules and Enzymes Flashcards
(26 cards)
Triacyglycerols AKA triglycerides AKA fats and oils
store energy ( and can give insulation and padding)
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major functions of lipids:
- phospholipids serve as a structural component of membranes;
- triacylglycerols store metabolic energy ana provide thermal insulation ana padding;
- steroids regulate metabolic activities; ana
- some fatty acids (eicosanoias) even serve as local hormones.
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Glycogen is found in liver and muscle cells. It is branched with alpha linkages.
a-1,4 in a line
a-1,6 at branch point
Starch is in plant chloroplasts: amylose is like glycogen but doesn’t have to be branched (alpha linkages like glycogen) and amylopectin is branched but differently (branched, different than glycogen)
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Liver regulates blood sugar. That’s why it can turn glycogen into glucose.
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Glucose is absorbed through facilitated diffusion. Insulin increases this rate. Some epithelial cells in digestive tract and proximal tubule of kidney absorb glucose through active transport.
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In absence of insulin, only neuronal cells and hepatic cells can absorb enough glucose through facilitated diffusion.
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Plants can also make cellulose (beta linkages, cellular structure) out of glucose, only bacteria can breakdown.
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Nucleotides:
- genetic material
- energy (ATP)
- second messengers (cAMP)
- coenzymes (FADH2 and NADH)
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Dehydration=condensation
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Enzyme catalysts are NOT reactants.
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Alpha amino acid: Amine (NH2) is attached to alpha carbon from carbonyl carbon.
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AA secondary structure: Alpha helices or B pleated sheets, where the connecting segments between the 2 strands can be in the same or opposite directions.
Both structures are reinforced with H bonds between the carbonyl O and a H in another AA.
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Hormones can be lipids (eicosanoids like prostaglandin) or proteins (insulin)
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Proteins are globular and structural.
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NITROGEN=protein
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Cytochromes: NEED heme + protein. Help in like , ETC. and hemoglobin is also a cytochrome.
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Conjugated proteins: Have a non-protein elements
Ex: cytochromes, glycoproteins, proteoglycans…
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Prosthetic=non protein
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Minerals purposes:
1-Add strength to a matrix
2-Transport ions in and out based off electrochemical gradients
3-Act as cofactors to help enzymes function (like found in heme, a prosthetic/cofactor group)
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Alteration with enzymes: increases enzyme specificity, destabilizes substrate (so lets it occur more efficiently) and when there are many substrates it orients the substrates relative to each other so the rxn occurs in optimal conditions (think quaternary)
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Turnover number is
the number of substrate molecules one active site can convert to product in a given unit of time when an enzyme solution is saturated with substrate.
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vitamins can be steroids, coenzymes
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secondary structure is defined by hydrogen bonding along the protein’s backbone (between O of carbonyl C and H of amino group), so partial double bond of amide group really helps here. while tertiary structure is defined by interactions between side groups
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Allosteric regulators are generally non-competitive, but some ARE competitive because some alter Km without affecting Vmax.
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