La deshidratación elimina una Molécula de agua y forma un Enlace nuevo. Polímero más largo Reacción de deshidratación en la síntesis de un polímero

Transcription

1 Figure 5-01

2 LE 5-2 Polímerto corto Monómero no unido La deshidratación elimina una Molécula de agua y forma un Enlace nuevo Polímero más largo Reacción de deshidratación en la síntesis de un polímero La hidrólisis agrega una Molécula de agua y rompe un enlace Hidrólisis de un polímero

3 LE 5-2a Polímero corto Monómero no unido La deshidratación elimina una Molécula de agua y forma un Enlace nuevo polímero más largo Reacción de deshidratación en la síntesis de un polímero

4 LE 5-2b La hidrólisis agrega una Molecula de agua y rompe un enlace Hidrólisis de un polímero

5 LE 5-3 Triose sugars (C 3 H 6 O 3 ) Pentose sugars (C 5 H 10 O 5 ) Hexose sugars (C 5 H 12 O 6 ) Glyceraldehyde Ribose Glucose Galactose Dihydroxyacetone Ribulose Fructose

6 LE 5-4 Forma lineal y anular Estructura anular abreviada

7 LE 5-4a Forma lineal Y anular

8 LE 5-4b Estructura anular abreviada

9 LE 5-5 Dehydration reaction in the synthesis of maltose 1 4 glycosidic linkage Glucose Glucose Maltose Dehydration reaction in the synthesis of sucrose 1 2 glycosidic linkage Glucose Fructose Sucrose

10 LE 5-5a Enlace Glucosídico 1 4 Glucose Glucose Maltose Reacción de deshidratación en la síntesis de maltosa

11 LE 5-5b Enlace Glucosídico 1 2 Glucose Fructose Sucrose Reacción de deshidratación en la síntesis de sacarosa

12 LE 5-6 Chloroplast Starch Mitochondria Glycogen granules 0.5 µm 1 µm Amylose Amylopectin Glycogen Starch: a plant polysaccharide Glycogen: an animal polysaccharide

13 LE 5-6a Chloroplast Starch 1 µm Amylose Amylopectin Almidón: un polisacárido vegetal

14 LE 5-6b Mitochondria Glycogen granules 0.5 µm Glycogen Glucógeno: un polisacárido animal

15 LE 5-7 a Glucose b Glucose a and b glucose ring structures Starch: 1 4 linkage of a glucose monomers. Cellulose: 1 4 linkage of b glucose monomers.

16 LE 5-7a a Glucose b Glucose Estructuras anulares de a y b glucosa

17 LE 5-7b Almidón: unión 1-4 de monómeros de a glucosa

18 LE 5-7c Celulosa: unión 1-4 de monómeros de b glucosa.

19 LE 5-8 Paredes celulares Microfibrillas de celulosa En una pared celular vegetal Microfibril 0.5 µm Plant cells Moléculas De celulosa Monómeros de B glucosa

20 Figure 5-09

21 LE 5-10 La estructura del Monómero de quitina. La quitina forma el exoesqueleto de los artrópodosla quitina se utiliza para fabricar un hili quirúrgico Esta cigarra está mudando despojándose de su Fuerte y flexible que se descomponedespués de que Viejo exoesqueleto y emergiendo como forma La herida o incisión se cura adulta

22 LE 5-11 Fatty acid (palmitic acid) Dehydration reaction in the synthesis of a fat Ester linkage Fat molecule (triacylglycerol)

23 LE 5-11a Ácido graso (ácido palmítico) Glycerol Reacción de deshidratación en la síntesis de una grasa

24 LE 5-11b Ester linkage Molécula de grasa (triacilglicerol)

25 LE 5-12 Stearic acid Saturated fat and fatty acid. Oleic acid Unsaturated fat and fatty acid. cis double bond causes bending

26 LE 5-12a Ácido esteárico Grasa saturada y ácido graso.

27 LE 5-12b Oleic acid Unsaturated fat and fatty acid. cis double bond causes bending

28 LE 5-13 Choline Phosphate Glycerol Fatty acids Cabeza hidófila Colas hidrófobas Fórmula estructural Modelo espacial Símbolo de fosfolípido

29 LE 5-13a Choline Phosphate Glycerol Fatty acids Structural formula Space-filling model

30 LE 5-13b Hydrophilic head Hydrophobic tails Phospholipid symbol

31 LE 5-14 Hydrophilic head WATER Hydrophobic tails WATER

32 Figure 5-15

33 Table 5-1

34 LE 5-UN78 a carbon Amino group Carboxyl group

35 LE 5-16 Substrate (sucrose) Glucose Enzyme (sucrose) Fructose

36 LE 5-17a Glycine (Gly) Alanine (Ala) Valine (Val) Leucine (Leu) Isoleucine (Ile) Nonpolar Methionine (Met) Phenylalanine (Phe) Tryptophan (Trp) Proline (Pro)

37 LE 5-17b Polar Serine (Ser) Threonine (Thr) Cysteine (Cys) Tyrosine (Tyr) Asparagine (Asn) Glutamine (Gln)

38 LE 5-17c Acidic Basic Electrically charged Aspartic acid (Asp) Glutamic acid (Glu) Lysine (Lys) Arginine (Arg) Histidine (His)

39 LE 5-18 Peptide bond Cadenas laterales Peptide bond Columna vertebral Amino acid (N-terminus) Carboxyl end (C-terminus)

40 LE 5-19 Groove A ribbon model Groove A space-filling model

41 LE 5-19a Groove A ribbon model

42 LE 5-19b Groove A space-filling model

43 LE H 3 N Amino end Amino acid subunits b pleated sheet a helix

44 LE 5-20a Amino end Amino acid subunits Carboxyl end

45 LE 5-20b b pleated sheet Amino acid subunits a helix

46 LE 5-20c Abdominal glands of the spider secrete silk fibers that form the web. The spiral strands (capture strands) are elastic, stretching in response to wind, rain, and the touch of insects. The radiating strands, made of dry silk fibers, maintain the shape of the web. Spider silk: a structural protein Containing b pleated sheets

47 LE 5-20d Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Disulfide bridge Ionic bond

48 LE 5-20db Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Disulfide bridge Ionic bond

49 LE 5-20e Polypeptide chain b Chains Iron Heme Polypeptide chain Collagen a Chains Hemoglobin

50 LE 5-21a 10 µm 10 µm Red blood cell shape Normal cells are full of individual hemoglobin molecules, each carrying oxygen. Red blood cell shape Fibers of abnormal hemoglobin deform cell into sickle shape.

51 LE 5-21b Normal hemoglobin Sickle-cell hemoglobin Primary structure Val His Leu Thr 4 Pro 5 Glu 6 Glu 7 Primary structure Val His Leu Thr 4 Pro 5 Val 6 Glu 7 Secondary and tertiary structures b subunit Secondary and tertiary structures Exposed hydrophobic region b subunit Quaternary structure Normal hemoglobin (top view) a b a b Quaternary structure Sickle-cell hemoglobin a b b a Function Molecules do not associate with one another; each carries oxygen. Function Molecules interact with one another to crystallize into a fiber; capacity to carry oxygen is greatly reduced.

52 LE 5-22 Denaturation Normal protein Denatured protein Renaturation

53 LE 5-23a Cap Hollow cylinder Chaperonin (fully assembled)

54 LE 5-23b Polypeptide Correctly folded protein Steps of Chaperonin Action: An unfolded polypeptide enters the cylinder from one end. The cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide. The cap comes off, and the properly folded protein is released.

55 LE 5-24a X-ray source Photographic film Diffracted X-rays X-ray beam X-ray diffraction pattern Crystal

56 LE 5-24b Nucleic acid Protein X-ray diffraction pattern 3D computer model

57 LE 5-25 DNA Synthesis of mrna in the nucleus mrna NUCLEUS CYTOPLASM mrna Movement of mrna into cytoplasm via nuclear pore Ribosome Synthesis of protein Polypeptide Amino acids

58 LE 5-26a 5 end Nucleoside Nitrogenous base Phosphate group Pentose sugar Nucleotide 3 end Polynucleotide, or nucleic acid

59 LE 5-26b Nitrogenous bases Pyrimidines Cytosine C Thymine (in DNA) T Uracil (in RNA) U Purines Adenine A Guanine G Pentose sugars Deoxyribose (in DNA) Ribose (in RNA) Nucleoside components

60 LE end 3 end Sugar-phosphate backbone Base pair (joined by hydrogen bonding) Old strands Nucleotide about to be added to a new strand 5 end New strands 3 end 5 end 5 end 3 end