Functional Groups Molec Biol

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amino group
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Terms in this set (54)
amino group
amines, proteins, act as base, attracts proton
Image: amino group
carboxyl group
carboxylic acids, acts as acid, tends to lose proton
Image: carboxyl group
carbonyl group
aldehydes and ketones, aldehydes tend to form larger compounds, some sugars
Image: carbonyl group
hydroxyl group
alcohols, high polarity, hydrogen bonds, can act as weak acid and lose proton
Image: hydroxyl group
phosphate group
organic phosphates, nucleic acids, lipids, molecules with many phosphates store chemical energy
Image: phosphate group
Sulfhydryl
thiols, when in proteins can form disulfide bonds that contribute to protein structure
Image: Sulfhydryl
write down what an amino terminus looks like
see picture
Image: write down what an amino terminus looks like
write down what an carboxy terminus looks like
see picture
Image: write down what an carboxy terminus looks like
what are the two termini in amino acids
carboxy and amino
what are the 5 types of interactions in tertiary structure
h bonds, ionic bonds, disulfide bonds, Van der Waals, hydrophobic interactions
what are the 6 functions of proteins?catalysis, transport, movement, structure, signals, defensewhat are the four levels of structure called and what do they meanprimary (order), secondary (alpha or beta through interactions), tertiary (3D order of things), quaternary (multiple pieces fitting together)what is the difference between DNA and RNA?RNA (single stranded, Uracil instead of Thymine, higher reactivity, less stable, two OH groups), DNA (double stranded, Thymine instead of Uracil, lower reactivity, only one OH group)adeninesee pictureThymidesee pictureUracilsee pictureGuaninesee pictureCytosinesee picturewhat are the two types of linkages between carbohydratesalpha, betawhat are the two possible locations of linkages in carbs1,4 or 1,6what are four(ish) structural differences that could result in different molecules (for carbs)location of linkage, order of monomers, types of linkages, combination of monomersHypertonicwhen comparing two solutions, the solution with the greater concentration of solutesHypotonicHaving a lower concentration of solute than another solutionIsotonicwhen the concentration of two solutions is the samewhy can integral proteins pass through the whole bilayer?they have nonpolar amino acids on their outsidestructural differences between channel and carrier proteinschannel (porous structure, doesn't move) carrier (shuttles, changes configuration)Starch structurePolysaccharide with unbranched chain of glucose with alpha linkagesGlycogen structureBranches have alpha(1,6) bonds; Linkages have alpha(1,4) bonds.Cellulose structureBeta 1,4 glycocidic linkages in a straight line.Chitin structurePolysaccharide with unbranched chain of glucose with beta linkages and nitrogen groupspeptidoglycan structuredisaccharide-NAG, NAM peptide chain-D-amino acids, Di-amino acidssaturated fatssingle bonds, tight together, more solidunsaturated fatshave double bonds, less tight, more fluidPhagocytosisA type of endocytosis in which a cell engulfs large particles or whole cellsKinesinA class of motor proteins that uses the chemical energy of ATP to "walk" toward the plus end of a microtubule. Used to transport vesicles, particles, organelles and chromosomes.DyeninMolecular motor protein that transports material retrograde to microtubule (+ to -)MyosinA protein present in muscle fibers that aids in contraction and makes up the majority of muscle fiberactin filamentsshape, movement, splitting of cellintermediate filamentsmaintain shape, anchor nucleus to organellesMicrotubulestracks for intracellular transport, moves cells,ribosomes functionprotein synthesisendomembrane system functionprotein synthesis and processingSmooth ER functionlipid synthesisrough ER functionprotein synthesisGolgi apparatus functionfurther processing of proteins, carbs, and lipidsLysosomestransport and break downperoxisomesoxidize fatty acids, ethanol, etc.microtubule organizing center...what is it?centrosome, minus end of microtubules∆Ggreater than 0 = endergonic (absorbs E), less than 0 = exergonic (releases E)∆S∆S >0 = more disorder, ∆S <0 = less disorder∆H∆H >0 = endothermic (absorbs heat), ∆H <0 = exothermic (releases heat)coenzymenonprotein necessary for enzyme functioncofactorsubstance (other than substrate) that is needed for the enzyme to workprosthetic groupsnon-polypeptide group bound to enzyme structure necessary for function

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