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Concept 5.4: Proteins have many structures,
resulting in a wide range of functions
• Proteins account for more than 50% of the dry
mass of most cells
• Protein functions include structural support,
storage, transport, cellular communications,
movement, and defense against foreign
substances
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Table 5-1
• Enzymes are a type of protein that acts as a
catalyst to speed up chemical reactions
• Enzymes can perform their functions
repeatedly, functioning as workhorses that
carry out the processes of life
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Fig. 5-16
Substrate
(sucrose)
Glucose
OH
Fructose
HO
Enzyme
(sucrase)
H2O
Polypeptides
• Polypeptides are polymers built from the
same set of 20 amino acids
• A protein consists of one or more polypeptides
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Amino Acid Monomers
• Amino acids are organic molecules with
carboxyl and amino groups
• Amino acids differ in their properties due to
differing side chains, called R groups
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-UN1
carbon
Amino
group
Carboxyl
group
Fig. 5-17
Nonpolar
Glycine
(Gly or G)
Valine
(Val or V)
Alanine
(Ala or A)
Methionine
(Met or M)
Leucine
(Leu or L)
Trypotphan
(Trp or W)
Phenylalanine
(Phe or F)
Isoleucine
(Ile or I)
Proline
(Pro or P)
Polar
Serine
(Ser or S)
Threonine
(Thr or T)
Cysteine
(Cys or C)
Tyrosine
(Tyr or Y)
Asparagine Glutamine
(Asn or N) (Gln or Q)
Electrically
charged
Acidic
Aspartic acid Glutamic acid
(Glu or E)
(Asp or D)
Basic
Lysine
(Lys or K)
Arginine
(Arg or R)
Histidine
(His or H)
Amino Acid Polymers
• Amino acids are linked by peptide bonds
• A polypeptide is a polymer of amino acids
• Polypeptides range in length from a few to
more than a thousand monomers
• Each polypeptide has a unique linear sequence
of amino acids
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Fig. 5-18
Peptide
bond
(a)
Side chains
Peptide
bond
Backbone
(b)
Amino end
(N-terminus)
Carboxyl end
(C-terminus)
Protein Structure and Function
• A functional protein consists of one or more
polypeptides twisted, folded, and coiled into a
unique shape
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Fig. 5-19
Groove
Groove
(a) A ribbon model of lysozyme
(b) A space-filling model of lysozyme
• The sequence of amino acids determines a
protein’s three-dimensional structure
• A protein’s structure determines its function
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-20
Antibody protein
Protein from flu virus
Four Levels of Protein Structure
• The primary structure of a protein is its unique
sequence of amino acids
• Secondary structure, found in most proteins,
consists of coils and folds in the polypeptide
chain
• Tertiary structure is determined by interactions
among various side chains (R groups)
• Quaternary structure results when a protein
consists of multiple polypeptide chains
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
• Primary structure, the sequence of amino
acids in a protein, is like the order of letters in a
long word
• Primary structure is determined by inherited
genetic information
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-21a
Primary Structure
1
+H
5
3N
Amino end
10
Amino acid
subunits
15
20
25
• The coils and folds of secondary structure
result from hydrogen bonds between repeating
constituents of the polypeptide backbone
• Typical secondary structures are a coil called
an  helix and a folded structure called a 
pleated sheet
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Fig. 5-21c
Secondary Structure
pleated sheet
Examples of
amino acid
subunits
helix
• Tertiary structure is determined by
interactions between R groups, rather than
interactions between backbone constituents
• These interactions between R groups include
hydrogen bonds, ionic bonds, hydrophobic
interactions, and van der Waals interactions
• Strong covalent bonds called disulfide
bridges may reinforce the protein’s structure
Animation: Tertiary Protein Structure
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-21f
Hydrophobic
interactions and
van der Waals
interactions
Polypeptide
backbone
Hydrogen
bond
Disulfide bridge
Ionic bond
• Quaternary structure results when two or
more polypeptide chains form one
macromolecule
• Collagen is a fibrous protein consisting of three
polypeptides coiled like a rope
• Hemoglobin is a globular protein consisting of
four polypeptides: two alpha and two beta
chains
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Fig. 5-21g
Polypeptide
chain
Chains
Iron
Heme
Chains
Hemoglobin
Collagen
Sickle-Cell Disease: A Change in
Primary Structure
• A slight change in primary structure can affect
a protein’s structure and ability to function
• Sickle-cell disease, an inherited blood disorder,
results from a single amino acid substitution in
the protein hemoglobin
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Fig. 5-22
Normal hemoglobin
Primary
structure
Sickle-cell hemoglobin
Primary
structure
Val His Leu Thr Pro Glu Glu
1
2
3
Secondary
and tertiary
structures
4
5
6
7
subunit
Secondary
and tertiary
structures
Val His Leu Thr Pro Val Glu
1
2
3
Exposed
hydrophobic
region
Quaternary
structure
Normal
hemoglobin
(top view)
Quaternary
structure
Sickle-cell
hemoglobin
Function
Molecules do
not associate
with one
another; each
carries oxygen.
Function
Molecules
interact with
one another and
crystallize into
a fiber; capacity
to carry oxygen
is greatly reduced.
10 µm
Red blood
cell shape
Normal red blood
cells are full of
individual
hemoglobin
moledules, each
carrying oxygen.
4
5
6
7
subunit
10 µm
Red blood
cell shape
Fibers of abnormal
hemoglobin deform
red blood cell into
sickle shape.
What Determines Protein Structure?
• In addition to primary structure, physical and
chemical conditions can affect structure
• Alterations in pH, salt concentration,
temperature, or other environmental factors
can cause a protein to unravel
• This loss of a protein’s native structure is called
denaturation
• A denatured protein is biologically inactive
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Fig. 5-23
Denaturation
Normal protein
Renaturation
Denatured protein
Protein Questions
• What type of bond joins two amino acids?
– Peptide, covalent
• Name the 2 common secondary structures of a
protein.
–  helix and  pleated sheet
• List the possible types of interactions at the
tertiary level of a protein.
– Hydrophobic / Hydrophillic, Van der Waals,
Hydrogen bonding, Disulfide bridge, ionic
bonding
Concept 5.5: Nucleic acids store and transmit
hereditary information
• The amino acid sequence of a polypeptide is
programmed by a unit of inheritance called a
gene
• Genes are made of DNA, a nucleic acid
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The Roles of Nucleic Acids
• There are two types of nucleic acids:
– Deoxyribonucleic acid (DNA)
– Ribonucleic acid (RNA)
• DNA provides directions for its own replication
• DNA directs synthesis of messenger RNA
(mRNA) and, through mRNA, controls protein
synthesis
• Protein synthesis occurs in ribosomes
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Fig. 5-26-3
DNA
1 Synthesis of
mRNA in the
nucleus
mRNA
NUCLEUS
CYTOPLASM
mRNA
2 Movement of
mRNA into cytoplasm
via nuclear pore
Ribosome
3 Synthesis
of protein
Polypeptide
Amino
acids
The Structure of Nucleic Acids
• Nucleic acids are polymers called
polynucleotides
• Each polynucleotide is made of monomers
called nucleotides
• Each nucleotide consists of a nitrogenous
base, a pentose sugar, and a phosphate group
• The portion of a nucleotide without the
phosphate group is called a nucleoside
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Fig. 5-27
5
end
Nitrogenous bases
Pyrimidines
5 C
3 C
Nucleoside
Nitrogenous
base
Cytosine (C)
Thymine (T, in DNA) Uracil (U, in RNA)
Purines
Phosphate
group
5 C
Sugar
(pentose)
Adenine (A)
Guanine (G)
(b) Nucleotide
3 C
Sugars
3
end
(a) Polynucleotide, or nucleic acid
Deoxyribose (in DNA)
Ribose (in RNA)
(c) Nucleoside components: sugars
Nucleotide Monomers
• Nucleoside = nitrogenous base + sugar
• There are two families of nitrogenous bases:
– Pyrimidines (cytosine, thymine, and uracil)
have a single six-membered ring
– Purines (adenine and guanine) have a sixmembered ring fused to a five-membered ring
• In DNA, the sugar is deoxyribose; in RNA, the
sugar is ribose
• Nucleotide = nucleoside + phosphate group
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Nucleotide Polymers
• Nucleotide polymers are linked together to build
a polynucleotide
• Adjacent nucleotides are joined by covalent
bonds that form between the –OH group on the
3 carbon of one nucleotide and the phosphate
on the 5 carbon on the next
• These links create a backbone of sugarphosphate units with nitrogenous bases as
appendages
• The sequence of bases along a DNA or mRNA
polymer is unique for each gene
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The DNA Double Helix
• A DNA molecule has two polynucleotides spiraling
around an imaginary axis, forming a double helix
• In the DNA double helix, the two backbones run in
opposite 5 → 3 directions from each other, an
arrangement referred to as antiparallel
• One DNA molecule includes many genes
• The nitrogenous bases in DNA pair up and form
hydrogen bonds: adenine (A) always with thymine
(T), and guanine (G) always with cytosine (C)
Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Fig. 5-28
5' end
3' end
Sugar-phosphate
backbones
Base pair (joined by
hydrogen bonding)
Old strands
Nucleotide
about to be
added to a
new strand
3' end
5' end
New
strands
5' end
3' end
5' end
3' end
Nucleic Acid Questions
• What are the “parts” of a nucleotide?
– Sugar, phosphate and nitrogen base
• Name the purines and pyrimidines.
– Purine – adenine and guanine
– Pyrimidine – thymine, cytosine and uracil
• What two molecules make up the uprights of
DNA?
– Nitrogen bases held together by hydrogen
bonds