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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