Beruflich Dokumente
Kultur Dokumente
Figure 5.1
HO 1 2 3 H HO H
HO 1 2 3 4 H
Longer polymer
Figure 5.2A (a) Dehydration reaction in the synthesis of a polymer
HO 1 2 3 4 H
HO 1 2 3 H HO H
Aldoses
H C OH H C OH HO C H HO C H
H H C OH H C OH HO C H
H C OH H C OH H C OH
Glyceraldehyde
H H C OH H C OH
Ribose H H
Glucose Galactose
H H H
H C OH H C OH H C OH
C O C O C O
Ketoses
H C OH H C OH HO C H
H H C OH H C OH
Dihydroxyacetone H C OH H C OH
H H C OH
Ribulose H
Figure 5.3 Fructose
Figure 5.4 (a) Linear and ring forms. Chemical equilibrium between the linear and ring
structures greatly favors the formation of rings. To form the glucose ring,
carbon 1 bonds to the oxygen attached to carbon 5.
Figure 5.5
1 m
Amylose Amylopectin
0.5 m
Glycogen
OH OH OH OH
(b) Starch: 1– 4 linkage of glucose monomers
CH2O CH2O
OH OH
H H
O O
O OH O OH
OH 1 4 O OH
HO OH
O O
CH2O CH2O
OH OH
H H
(c) Cellulose: 1– 4 linkage of glucose monomers
Figure 5.7 A–C
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
– Is a major component of the tough walls that
enclose plant cells
About 80 cellulose
Cellulose microfibrils molecules associate
in a plant cell wall Microfibril to form a microfibril, the
Cell walls main architectural unit
of the plant cell wall.
0.5 m
Plant cells
CH2OH OH CH2OH OH
O O O O
OH OH OH OH
O O O O O
O CH OH OH CH2OH
H
2 Cellulose
CH2OH OH CH2OH OH molecules
O O O O
OH OH OH OH
Parallel cellulose molecules are O O O O O
O CH OH OH CH2OH
held together by hydrogen H
2
Figure 5.9
(a) The structure of the (b) Chitin forms the exoskeleton (c) Chitin is used to make a
chitin monomer. of arthropods. This cicada strong and flexible surgical
is molting, shedding its old thread that decomposes after
exoskeleton and emerging the wound or incision heals.
Figure 5.10 A–C in adult form.
Stearic acid
Oleic acid
Fatty acids
Hydrophilic
head
Hydrophobic
tails
(c) Phospholipid
(a) Structural formula (b) Space-filling model
Figure 5.13 symbol
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
• The structure of phospholipids
– Results in a bilayer arrangement found in cell
membranes
WATER
Hydrophilic
head
WATER
Hydrophobic
tail
Figure 5.14
H3C CH3
CH3 CH3
CH3
Figure 5.15 HO
Glucose
Enzyme
OH (sucrase)
H2O
Fructose
H O
• A protein
– Consists of one or more polypeptides
CH3
CH3 CH3
CH3
CH2
S
H2C CH2
NH O
CH2
H2N C C
CH2 O CH2 CH2 O–
O O H
H3N+ C C H3N+ C C H3N+ C C
O– O– O–
H H H
Methionine (Met) Phenylalanine (Phe) Tryptophan (Trp) Proline (Pro)
Figure 5.17
Acidic Basic
(a) H2O
OH
DESMOSOMES
DESMOSOMES Side
OH SH
Peptide chains
CH2 CH2 bond CH2
H H H
H N C C N C C N C C OH Backbone
H O H O H O
Groove
Groove
Amino LeuPro
Cys LysSeu
Glu
subunits
end Met
Val
Lys
Val
Leu
Asp
AlaVal Arg Gly
Ser
Pro
Ala
Glu Lle
Asp
Thr
Lys
Ser
Lys Trp Tyr
Leu Ala
Gly
lle
Ser
ProPhe
His Glu
His
Ala
Glu
Val
Ala Thr PheVal
Asn
lle
Thr
Asp Tyr Ala
Arg
Ser Arg Ala
Gly Pro
Leu
Leu
Ser
Pro
SerTyr
Tyr
Thr Ser
Thr
Ala
Val o
Val LysGlu c
Thr
AsnPro o–
R R R R
O C O O C O H
C H H H C
H C N HC H H
C N HC N N C NH C N C N HC N
H H C H O C H
C O C O O C
R R R
R H R H
C C
N H O C N H O C
N H
O C O C
N H
helix
H C R H C H C R H C R
R
N H O C N H
O C
O C N H O C N H
C C
R H R H
Figure 5.20
Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings
• Tertiary structure
– Is the overall three-dimensional shape of a
polypeptide
– Results from interactions between amino acids
and R groups Hydrophobic
interactions and
CH van der Waals
CH22
CH
H3C CH3 interactions
O
Hyrdogen H H3C CH3 Polypeptide
bond O CH backbone
HO C
CH2 CH2 S S CH2
Disulfide bridge
O
CH2 NH3+ -O C CH2
Ionic bond
Polypeptide
chain
Collagen
Chains
Iron
Heme
Chains
Hemoglobin
• Sickle-cell disease
❑caused by the substitution of one amino acid (valine)
for the normal one (glutamic acid) at the position of the
sixth amino acid in the primary structure of hemoglobin
Hollow
cylinder
Chaperonin Steps of Chaperonin 2 The cap attaches, causing 3 The cap comes
(fully assembled) Action: the cylinder to change shape in off, and the properly
1 An unfolded poly- such a way that it creates a folded protein is
peptide enters the hydrophilic environment for the released.
Figure 5.23 cylinder from one end. folding of the polypeptide.
1 Synthesis of
mRNA in the nucleus mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into cytoplasm Ribosome
via nuclear pore
3 Synthesis
of protein
Amino
Figure 5.25 Polypeptide acids
Sugar-phosphate
backbone
Base pair (joined by
hydrogen bonding)
Old strands
Nucleotide
about to be
added to a
new strand
A 3’ end
5’ end
3’ end New
strands
• Organization
– Is the key to the chemistry of life