fig. 3-6, p. 38
DESCRIPTION
Fig. 3-6, p. 38. Fig. 3-5, p. 37. one of the estrogens. testosterone. Fig. 3-4, p. 37. glucose. fructose. sucrose. c Formation of a sucrose molecule. Fig. 3-6, p. 38. Fig. 3-8, p. 39. c Glycogen. In animals, this - PowerPoint PPT PresentationTRANSCRIPT
![Page 1: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/1.jpg)
Fig. 3-6, p. 38
![Page 2: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/2.jpg)
Fig. 3-5, p. 37
![Page 3: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/3.jpg)
one of the estrogens
Fig. 3-4, p. 37
testosterone
![Page 4: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/4.jpg)
glucose fructose
sucrose
Fig. 3-6, p. 38
c Formation of a sucrose molecule
![Page 5: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/5.jpg)
Fig. 3-8, p. 39
![Page 6: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/6.jpg)
Fig. 3-8, p. 39
c Glycogen. In animals, thispolysaccharide is a storage form for excess glucose. It is especially abundant in the liver and muscles of highly active animals, including fishes and people.
Structure of cellulose
![Page 7: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/7.jpg)
glycerol
three fatty acid tails Triglyceride, a neutral fatFig. 3-11, p. 40
![Page 8: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/8.jpg)
Fig. 3-12, p. 41
![Page 9: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/9.jpg)
hydrophilic head
two hydrophilic tails
Fig. 3-13, p. 41
![Page 10: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/10.jpg)
Fig. 3-13, p. 41
c Cell membrane section
![Page 11: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/11.jpg)
Fig. 3-15, p. 42
carboxylgroup
aminogroup
![Page 12: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/12.jpg)
Fig. 3-17, p. 43
a Protein primarystructure: Aminoacids bonded in apolypeptide chain.
![Page 13: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/13.jpg)
Fig. 3-17, p. 43
b Protein secondarystructure: A coiled(helical) or sheetlikearray, held in placeby hydrogen bonds( dotted lines) betweendifferent parts of thepolypeptide chain.
helical coil sheet
![Page 14: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/14.jpg)
Fig. 3-17, p. 43
c Protein tertiary structure: A chain’s coiled parts, sheetlikearrays, or both have folded and twisted into stable, functionaldomains, including clusters, pockets, and barrels.
barrel
![Page 15: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/15.jpg)
Fig. 3-17, p. 43
d Protein quaternarystructure: Many weakinteractions hold twoor more polypeptidechains together asa single molecule.
![Page 16: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/16.jpg)
alpha globin
beta globin beta globin
Fig. 3-18, p. 44
alpha globin
b Hemoglobin is one of the proteins with quaternary structure. Itconsists of four globin molecules held together by hydrogen bonds.To help you distinguish among them, the two alpha globin chainsare shown here in green, and the two beta globins are in brown.
![Page 17: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/17.jpg)
Fig. 3-19, p. 45
VALINE HISTIDINE LEUCINE GLUTAMATEVALINETHREONINE PROLINE
sickle cell
normal cell
b One amino acid substitution results in theabnormal beta chain in HbS molecules. Insteadof glutamate, valine was added at the sixthposition of the polypeptide chain.
c Glutamate has an overall negative charge; valine has no net charge. At low oxygen levels, this difference gives rise to a water-repellent, sticky patch on HbS molecules. They stick togetherbecause of that patch, forming rodshaped clumps that distort normally rounded red blood cells into sickle shapes. (A sickle is a farm tool that has a crescent-shaped blade.)
![Page 18: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/18.jpg)
Fig. 3-20, p. 46
three phosphate groups
base (blue)
sugar (orange)
![Page 19: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/19.jpg)
Fig. 3-21, p. 46
![Page 20: Fig. 3-6, p. 38](https://reader035.vdocuments.site/reader035/viewer/2022062315/56815dff550346895dcc411d/html5/thumbnails/20.jpg)
Fig. 3-22, p. 47
covalentbonding incarbonbackbone
hydrogen bondingbetween bases