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Figure 5-01

LE 5-2

Polímerto corto Monómero no unido

La deshidratación elimina una

Molécula de agua y forma un

Enlace nuevo

Reacción de deshidratación en la síntesis de un polímero

Polímero más largo

La hidrólisis agrega una

Molécula de agua y rompe un

enlace

Hidrólisis de un polímero

LE 5-2a

Polímero corto Monómero no unido

La deshidratación elimina una

Molécula de agua y forma un

Enlace nuevo

Reacción de deshidratación en la síntesis de un polímero

´polímero más largo

LE 5-2b

La hidrólisis agrega una

Molecula de agua y rompe un

enlace

Hidrólisis de un polímero

LE 5-3

Triose sugars

(C3H6O3)

Glyceraldehyde

Pentose sugars

(C5H10O5)

Ribose

Hexose sugars

(C5H12O6)

Glucose Galactose

Dihydroxyacetone

Ribulose

Fructose

LE 5-4

Forma lineal y anular Estructura anular

abreviada

LE 5-4a

Forma lineal

Y anular

LE 5-4b

Estructura anular abreviada

LE 5-5

Glucose

Maltose

Fructose Sucrose

Glucose Glucose

Dehydration

reaction in the

synthesis of maltose

Dehydration

reaction in the

synthesis of sucrose

1–4glycosidic

linkage

1–2glycosidic

linkage

LE 5-5a

MaltoseGlucose Glucose

Reacción de deshidra-

tación en la síntesis de

maltosa

EnlaceGlucosídico

1 – 4

LE 5-5b

Glucose Fructose Sucrose

Reacción de deshidrata-

ción en la síntesis de

sacarosa

EnlaceGlucosídico

1 – 2

LE 5-6

Chloroplast Starch Mitochondria Glycogen granules

0.5 µm

1 µm

Amylose

Starch: a plant polysaccharide

Amylopectin Glycogen

Glycogen: an animal polysaccharide

LE 5-6a

Chloroplast Starch

1 µm

Amylose

Almidón: un polisacárido vegetal

Amylopectin

LE 5-6b

Mitochondria Glycogen granules

0.5 µm

Glycogen

Glucógeno: un polisacárido animal

LE 5-7

a Glucose

a and b glucose ring structures

b Glucose

Starch: 1–4 linkage of a glucose monomers.

Cellulose: 1–4 linkage of b glucose monomers.

LE 5-7a

a Glucose

Estructuras anulares de a y b glucosa

b Glucose

LE 5-7b

Almidón: unión 1-4 de monómeros de a glucosa

LE 5-7c

Celulosa: unión 1-4 de monómeros de b glucosa.

LE 5-8

Moléculas

De celulosa

Microfibrillas de celulosa

En una pared celular vegetal

Paredes celulares Microfibril

Plant cells

0.5 µm

Monómeros de

B glucosa

Figure 5-09

LE 5-10

La quitina forma el exoesqueleto de los artrópodosEsta cigarra está mudando despojándose de su Viejo exoesqueleto y emergiendo como forma adulta

La quitina se utiliza para fabricar un hili quirúrgicoFuerte y flexible que se descomponedespués de queLa herida o incisión se cura

La estructura del Monómero de quitina.

LE 5-11

Dehydration reaction in the synthesis of a fat

Ester linkage

Fat molecule (triacylglycerol)

Fatty acid

(palmitic acid)

LE 5-11a

Reacción de deshidratación en la síntesis de una grasa

Glycerol

Ácido graso

(ácido palmítico)

LE 5-11b

Ester linkage

Molécula de grasa (triacilglicerol)

LE 5-12

Saturated fat and fatty acid.

Unsaturated fat and fatty acid.

Stearic acid

Oleic acid

cis double bondcauses bending

LE 5-12a

Grasa saturada y ácido graso.

Ácido esteárico

LE 5-12b

Unsaturated fat and fatty acid.

Oleic acid

cis double bondcauses bending

LE 5-13

Fórmula estructural Modelo espacial Símbolo de fosfolípido

Cabeza

hidófila

Colashidrófobas

Fatty acids

Choline

Phosphate

Glycerol

LE 5-13a

Structural formula Space-filling model

Fatty acids

Choline

Phosphate

Glycerol

LE 5-13b

Phospholipid symbol

Hydrophilic

head

Hydrophobictails

LE 5-14

WATERHydrophilic

head

Hydrophobic

tailsWATER

Figure 5-15

Table 5-1

LE 5-UN78

Amino

group

Carboxyl

group

a carbon

LE 5-16

Substrate

(sucrose)

Enzyme

(sucrose)

Fructose

Glucose

LE 5-17a

Isoleucine (Ile)

Methionine (Met) Phenylalanine (Phe) Tryptophan (Trp) Proline (Pro)

Leucine (Leu)Valine (Val)Alanine (Ala)

Nonpolar

Glycine (Gly)

LE 5-17b

Asparagine (Asn) Glutamine (Gln)Threonine (Thr)

Polar

Serine (Ser) Cysteine (Cys) Tyrosine (Tyr)

LE 5-17c

Electricallycharged

Aspartic acid (Asp)

Acidic Basic

Glutamic acid (Glu) Lysine (Lys) Arginine (Arg) Histidine (His)

LE 5-18

Peptidebond

Cadenas laterales

Columna vertebral

Amino acid(N-terminus)

Carboxyl end(C-terminus)

Peptidebond

LE 5-19

A ribbon model

Groove

Groove

A space-filling model

LE 5-19a

A ribbon model

Groove

LE 5-19b

Groove

A space-filling model

LE 5-20

Amino acidsubunits

b pleated sheet

+H3NAmino end

a helix

LE 5-20a

Amino acidsubunits

Carboxyl end

Amino end

LE 5-20b

Amino acid

subunits

b pleated sheet

a helix

LE 5-20c

Abdominal glandsof the spidersecrete silk

fibers that formthe web.

The radiatingstrands, made

of dry silk fibers,maintain the

shape of the web.

Spider silk: a structural proteinContaining b pleated sheets

The spiral strands(capture strands) areelastic, stretching in response to wind,rain, and the touchof insects.

LE 5-20d

Hydrophobic

interactions and

van der Waals

interactions

Polypeptide

backbone

Disulfide bridge

Ionic bond

Hydrogen

bond

LE 5-20db

Hydrophobic

interactions and

van der Waals

interactions

Polypeptide

backbone

Disulfide bridge

Ionic bond

Hydrogen

bond

LE 5-20e

b Chains

a ChainsHemoglobin

Iron

Heme

CollagenPolypeptide chain

Polypeptidechain

LE 5-21a

Red blood

cell shapeNormal cells are

full of individual

hemoglobin

molecules, each

carrying oxygen.

10 µm 10 µm

Red blood

cell shape

Fibers of abnormal

hemoglobin deform

cell into sickle

shape.

LE 5-21b

Primary

structure

Secondary

and tertiary

structures

1 2 3

Normal hemoglobin

Val His Leu

4

Thr

5

Pro

6

Glu Glu

7Primary

structure

Secondary

and tertiary

structures

1 2 3

Sickle-cell hemoglobin

Val His Leu

4

Thr

5

Pro

6

Val Glu

7

Quaternary

structure

Normal

hemoglobin

(top view)

a

b

b

b

b

a

a

a

Function Molecules do

not associate

with one

another; each

carries oxygen.

Quaternary

structure

Sickle-cell

hemoglobin

Function Molecules

interact with

one another to

crystallize into

a fiber; capacity

to carry oxygen

is greatly reduced.

Exposed

hydrophobic

regionb subunit b subunit

LE 5-22

Denaturation

Renaturation

Denatured proteinNormal protein

LE 5-23a

Chaperonin

(fully assembled)

Hollow

cylinder

Cap

LE 5-23b

Polypeptide

Correctly

folded

protein

An unfolded poly-

peptide enters the

cylinder from one

end.

Steps of Chaperonin

Action:The cap comes

off, and the

properly folded

protein is released.

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.

LE 5-24a

Photographic film

Diffracted X-rays

X-ray

sourceX-ray

beam

X-ray

diffraction pattern

Crystal

LE 5-24b

Nucleic acid

3D computer modelX-ray diffraction pattern

Protein

LE 5-25

NUCLEUS

DNA

CYTOPLASM

mRNA

mRNA

Ribosome

Amino

acids

Synthesis of

mRNA in the nucleus

Movement of

mRNA into cytoplasm

via nuclear pore

Synthesis

of protein

Polypeptide

LE 5-26a

5 end

3 end

Nucleoside

Nitrogenous

base

Phosphate

group

Nucleotide

Polynucleotide, or

nucleic acid

Pentose

sugar

LE 5-26b

Nitrogenous bases

Pyrimidines

Purines

Pentose sugars

Cytosine

C

Thymine (in DNA)

T

Uracil (in RNA)

U

Adenine

A

Guanine

G

Deoxyribose (in DNA)

Nucleoside components

Ribose (in RNA)

LE 5-27

Sugar-phosphate

backbone

3 end5 end

Base pair (joined by

hydrogen bonding)

Old strands

Nucleotide

about to be

added to a

new strand

5 end

New strands

3 end

5 end3 end

5 end