1. Biological Macromolecules
Structure and Function of
Carbohydrates, Nucleic Acids,
Proteins, Lipids

2. Cells as chemical reactors
 Living organisms obey the laws of
chemistry and physics
 Can think of cells as complex chemical reactors in
which many different chemical reactions are
proceeding at the same time
 All cells more similar then different if
looked at on the inside!
 Strip away the exterior and we see that all cells need
to accomplish similar tasks and in a broad sense they
use the same mechanisms (chemical reactions)
 Reflects a singular origin of all extant living things!

3. Similarities among all types of cells
 All cells use nucleic acids (DNA) to store information
 RNA viruses, but not true cells
(incapable of autonomous replication)
 All cells use proteins as catalysts (enzymes) for
chemical reactions
 A few examples of RNA based enzymes, which may reflect
primordial use of RNA
 All cells use lipids for membrane components
 Different types of lipids in different types of cells
 All cells use carbohydrates for cell walls (if present),
recognition, and energy generation
 All cells use nucleic acids (RNA) to access
stored information

4. Macromolecules
 Large Molecules
 Macromolecules are formed when
monomers are linked together to form
longer chains called polymers.
 The same process of making and breaking
polymers is found in all living organisms.

5.  Consider some generic monomers with OH groups on their ends.
 These monomers can be linked together by a process called
dehydration synthesis (also called a condensation reaction) in
which a covalent bond is formed between the two monomers while
a water molecule is also formed from the OH groups.
 This reaction is catalyzed by a polymerase enzyme.
 This same type of condensation reaction can occur to form many
kinds of polymers, from proteins to carbohydrates, nucleic acids to
triglycerides.
Condensation Reaction

6. Hydrolysis Reactions
 Polymers of all sorts can be broken apart
by hydrolysis reactions. In hydrolysis the
addition of a water molecule (with the help
of a hydrolase enzyme) breaks the
covalent bond holding the monomers
together.

7. Macromolecules
 Biotechnology often concerned with the
manipulation of cells through the manipulation
of the macromolecules contained within those
cells
 DNA
 Proteins
 Lipids & Carbohydrates (indirectly)

8.  Biologically important macromolecules are
“polymers” of smaller subunits
 Created through condensation reactions
Carbohydrates : simple sugars
Lipids : CH2 units
Proteins : amino acids
Nucleic acids : nucleotides
Macromolecule Subunit

9. Where do the subunits come from?
 All cells need a source of the atomic components of the
subunits
 (C, O, H, N, P, and a few other trace elements )
 Some cells can synthesize all of the subunits given these
atomic components and an energy source
 Some cells can obtain these subunits from external sources
 Some cells can convert other compounds into these subunits
 We will discuss further in section on metabolism and cell
growth

10. Carbohydrates
 All have general formula CnH2nOn (hydrates
(H2O) of carbon)
 A variety of functions in the cell
 Large cross-linked carbohydrates make up the
rigid cell wall of plants, bacteria, and insects
 In animal cells carbohydrates on the exterior
surface of the cell serve a recognition and
identification function
 A central function is energy storage
and energy production !

11. Carbohydrates
 Carbohydrates are always composed of
carbon, hydrogen and oxygen molecules
 Monosaccharides typically have five or
six carbon atoms.
 Monosaccharides can, such as the ribose
and deoxyribose of RNA and DNA, can
serve very important functions in cells.

12. Carbohydrates
 Condensation reactions form covalent
bonds between monosaccharides, called
glycosidic linkages.
 Monosaccharides are the monomers for
the larger polysaccharides.
 Polysaccharides play various roles, from
energy storage (starch, glycogen) to
structure (cellulose).

13. Carbohydrates
 Cell structure:
 Cellulose, LPS, chitin
Cellulose in plant cell walls Lipopolysaccharides (LPS)
in bacterial cell wall
Chitin in exoskeleton

14. Carbohydrate Structure
Monosaccharides may also form part of
other biologically important molecules

15. Carbohydrate Structure
 Complex carbohydrates built from simple sugars
 Most often five (pentose) or six (hexose) carbon
sugars
 Numerous –OH (hydroxy) groups can form many
types of “cross links”
 Can result in very complex and highl;y cross
linked structures ( cellulose, chitin, starch, etc.)

16. Carbohydrate Structure
A Few Examples
 Triose (3 carbon)
 Glyceraldehyde
 Pentose (5 carbon)
 Ribose

17. Carbohydrate Structure
Example of two hexoses
 Glucose Galactose
 What’s the difference? Both are C6H12O6
 They are isomers of one another!
 Same formula, but different structure (3D-shape).

18. Carbohydrate Structure
 Monosacharides can be joined to one another to form
disaccharides, trisaccharides, ……..polysaccharides
 Saccharide is a term derived from the Latin for sugar (origin = "sweet sand")
 Carbohydrates classified according to the number of
saccharide units they contain.
 A monosaccharide contains a single carbohydrate, over
200 different monosaccharides are known.
 A disaccharide gives two carbohydrate units on
hydrolysis.
 An oligosaccharide gives a "few" carbohydrate units on
hydrolysis, usually 3 to 10.
 A polysaccharide gives many carbohydrates on
hydrolysis, examples are starch and cellulose.

19. Carbohydrate Structure
Ring (cyclic) form
Pentoses and hexoses are capable of forming ring (cyclic) structures.
An equilibrium exists between the ring and open form.
Linear form

20. Carbohydrate Structure
 Monosaccharides can link
to form disaccharides
Glucose Fructose Sucrose
+

21. Complex Carbohydrates
 Cellulose
Most abundant carbohydrate on the planet!
 Component of plant cell walls
 Indigestible by animals
 β 1-4 bonds
 Starch
 Energy storage molecule in plants
 Can be digested by animals
 α 1-6 bonds

22. Cellulose
 Cellulose is a linear
polysaccharide in which some
1500 glucose rings link together.
It is the chief constituent of cell
walls in plants.
 Human digestion cannot break
down cellulose for use as a food,
animals such as cattle and
termites rely on the energy
content of cellulose. They have
protozoa and bacteria with the
necessary enzymes in their
digestive systems. Only animals
capable of breaking down
cellulose are tunicates.

23. Starches
 Starches are carbohydrates in which
300 to 1000 glucose units join
together. It is a polysaccharide used
to store energy for later use. Starch
forms in grains with an insoluble
outer layer which remain in the cell
where it is formed until the energy is
needed. Then it can be broken down
into soluble glucose units. Starches
are smaller than cellulose units, and
can be more readily used for energy.
In animals, the equivalent of starch
is glycogen, which can be stored in
the muscles or in the liver for later
use.
 α-1,6 bonds

24. Complex Carbohydrates
 Glycogen
 Branched chain polymer of glucose
 Animal energy reserve
 Found primarily in liver and muscle
 α 1-4 & α 1-6 bonds

25.  Glycogen

26. polysaccharides can be linked to other
molecules to form glyco-proteins and glyco-lipids

27. Glycoproteins
Some examples
 Polysaccharide component of antibodies has major effect
on antibody function
 Polysaccharides attached to proteins on surface of red
blood cells (RBC) determine blood type (A,B,O)
 Polysaccharides are attached to proteins in the Golgi
apparatus through a process of post-translational
modification
 Different types of cells do different post-tranlational
modifications
 More about this later

28. Glycolipids
 Polysaccharides can also be attached to lipid molecules
•An outer-membrane constituent of gram negative bacteria, LPS, which includes O-antigen, a
core polysaccharide and a Lipid A, coats the cell surface and works to exclude large
hydrophobic compounds such as bile salts and antibiotics from invading the cell. O-antigen are
long hydrophilic carbohydrate chains (up to 50 sugars long) that extend out from the outer
membrane while Lipid A (and fatty acids) anchors the LPS to the outer membrane.

29. Glycolipids
 Polysaccharides (blue)
are also used in animal
cells to link surface
proteins and lipid
anchors to the
membrane.

30. Lipids
 Lipids
 Fatty acids (Polymers of CH2 units)
 Glycerol
 Triglycerides
 Other subunits (phosphate, choline, etc) may be attached
to yield “phospholipids”
 Charged phosphate groups will create a polar molecule with a
hydrophobic (nonpolar) end and a hydrophillic (polar) end

31. Lipids
 Lipids constitute a very diverse group of molecules that all share
the property of being hydrophobic.
 Fats and oils are lipids generally associated with energy storage.
 Fatty acids, which make up fats and oils, can be saturated or
unsaturated, depending on the absence or presence of double
bonded carbon atoms.
 Other types of lipids are used for a other purposes, including
pigmentation (chlorophyll, carotenoids), repelling water (cutin,
suberin, waxes) and signaling (cholesterol and its derivatives).

32. Lipids
 Lipids are joined together by
ester linkages.
 Triglyceride is composed of 3 fatty acid
and 1 glycerol molecule
 Fatty acids attach to Glycerol by covalent
ester bond
 Long hydrocarbon chain of each fatty acid
makes the triglyceride molecule nonpolar
and hydrophobic

33. Lipids

35. Lipids

36. Phospholipids

37. Lipids
Function
 Energy Storage
 Triglycerides
 Cell membranes and cell compartments
 Bi-layer structure
 Outer or plasma membrane
 Nuclear membrane
 Internal structures
 Er, Golgi, Vesicles, etc.

38. Phospholipid bilayer
Hydrophillic heads
Hydrophobic tails

39. Steroids

40. Proteins
 Proteins serve many essential roles in the cell
 Polymers of amino acids
 20 naturally occurring amino acids
 A few modified amino acids are used
 The large number of amino acids allows huge diversity
in amino acid sequence
N = # of amino acids in a protein
N20
= # of possible combinations

41. Proteins
 Proteins consist of one or more polymers called
polypeptides, which are made by linking
amino acids together with peptide linkages.
 Peptide linkages are formed through
condensation reactions.
 All proteins are made from the same 20 amino acids.
 Different amino acids have different chemical
properties.

42. Proteins
 Protein’s primary structure largely
determines its secondary, tertiary (and
quaternary) structure.
 Proteins subjected to extreme conditions
(large changes in pH, high temperatures,
etc.) often denature.
 Proteins act as enzymes, and catalyze very
specific chemical reactions.

43. Protein Function
Some examples
 Structure- form structural components of the cell including:
 Cytoskeleton / nuclear matrix / tissue matrix
 Lamins, collagen, keratin…….
 Movement - Coordinate internal and external movement of cells,
organells, tissues, and molecules.
 Muscle contraction, chromosome separation, flagella………
 Micro-tubueles, actin, myosin
 Transport-regulate transport of molecules into and out of the cell / nucleus
/ organelles.
 Channels, receptors, dynin, kinesin
 Communication-serve as communication molecules between different
organelles, cells, tissues, organs, organisms.
 Hormones

44. Protein Function
Some examples
 Chemical Catalyst – serves to make possible all of the
chemical reactions that occur within the cell.
 Enzymes (thousands of different enzymes)
 Defense-recognize self and non-self, able to destroy
foreign entities (bacteria, viruses, tissues).
 Antibodies, cellular immune factors
 Regulatory-regulates cell proliferation, cell growth, gene
expression, and many other aspects of cell and organism
life cycle.
 Checkpoint proteins, cyclins, transcription factors

45. Protein Structure
 Polymers of 20 amino acids
 All amino acids have a
Common “core”
 Amino end (N end)
 Acid end (C end, carboxy
end)
 Linked by peptide bond
 20 different side chains

46. Properties of amino acids
 amino acids:
acidic
basic
hydrophobic
 Amino acids all have
The same basic structure
 Chemical properties of the
amino acids yield
properties of the protein!

47. Properties of amino acids

48. Protein Structure
 The 3-D shape and properties of the protein
determine its function.
 Shape and properties of protein determined by
interactions between individual amino acid
components.
 Four “levels” of protein structure
 Primary (Io
), secondary (IIo
), tertiary (IIIo
), and
quaternary (IVo
) (sometimes).

49. Levels of Protein Structure
 I0
(primary) structure
 Linear order of amino acids in a protein:
 1 A A S X D X S L V E V H X X V F I V P P X I L Q A V V S I A
 31 T T R X D D X D S A A A S I P M V P G W V L K Q V X G S Q A
 61 G S F L A I V M G G G D L E V I L I X L A G Y Q E S S I X A
 91 S R S L A A S M X T T A I P S D L W G N X A X S N A A F S S
 121 X E F S S X A G S V P L G F T F X E A G A K E X V I K G Q I
 151 T X Q A X A F S L A X L X K L I S A M X N A X F P A G D X X
 181 X X V A D I X D S H G I L X X V N Y T D A X I K M G I I F G
 211 S G V N A A Y W C D S T X I A D A A D A G X X G G A G X M X
 241 V C C X Q D S F R K A F P S L P Q I X Y X X T L N X X S P X
 271 A X K T F E K N S X A K N X G Q S L R D V L M X Y K X X G Q
 301 X H X X X A X D F X A A N V E N S S Y P A K I Q K L P H F D
 331 L R X X X D L F X G D Q G I A X K T X M K X V V R R X L F L
 361 I A A Y A F R L V V C X I X A I C Q K K G Y S S G H I A A X
 391 G S X R D Y S G F S X N S A T X N X N I Y G W P Q S A X X S
 421 K P I X I T P A I D G E G A A X X V I X S I A S S Q X X X A
 451 X X S A X X A
Single letter code for amino acids, also a three letter code.
Refer to your genetic code handout.

50. Levels of Protein Structure
Primary Structure
 Amino acids combine to form a chain
 Each acid is linked by a peptide bond
 Io
structure by itself does not provide a lot of
information.

51. Protein Structure
 II0
(secondary) structure
 Based on local interactions between amino acids
 Common repeating structures found in proteins. Two
types: alpha-helix and beta-pleated sheet.
 In an alpha-helix the polypeptide main chain makes up
the central structure, and the side chains extend out
and away from the helix.
 The CO group of one amino acid (n) is hydrogen
bonded to the NH group of the amino acid four
residues away (n +4).
 Can predict regions of secondary structure

52. Ribbon Diagram
α-helical regions

53. Beta sheet
 Two types parallel
and anti-parallel

54. Beta Sheet ribbon diagram
antiparallel
parallel

55. Protein Structure
 III0
(tertiary structure)
 Complete 3-D structure
of protein (single
polypeptide)
Chymotrypsin with inhibitor
hexokinase

56. Protein Structure
 IV0
(quaternary)
structure
 Not all proteins have
IV0
structure
 Only if they are made
of multiple polypeptide
chains

57. Nucleic Acid
 DNA is transmitted
from generation to
generation with
high fidelity, and
therefore represents
a partial picture of
the history of life.

58. Nucleic Acid
 Two types of nucleic acids:
 DNA
 RNA
 DNA stores the genetic information of organisms; RNA is used to transfer that
information into the amino acid sequences of proteins.
 DNA and RNA are polymers composed of subunits called nucleotides.
 Nucleotides consist of a five-carbon sugar, a phosphate group and a nitrogenous
base.
 Five nitrogenous bases found in nucleotides:
 the purines
 adenine (A)
 guanine (G)
 the pyrimidines
 cytosine (C)
 thymine (T) (DNA only)
 uracil (U) (RNA only)

59. Nucleic Acids
 DNA –deoxyribonucleic acid
 Polymer of deoxyribonucleotide triphosphate (dNTP)
 4 types of dNTP (ATP, CTP, TTP, GTP)
 All made of a base + sugar + triphosphate
 RNA –ribonucleic acid
 Polymer of ribonucleotide triphosphates (NTP)
 4 types of NTP (ATP, CTP, UTP, GTP)
 All made of a base + sugar + triphosphate
 So what’s the difference?
 The sugar (ribose vs. deoxyribose) and one base (UTP vs.
TTP)

61. Function
 Nucleic Acids
 Information Storage
 DNA / mRNA
 Information transfer / Recognition
 rRNA / tRNA / snRNA
 Regulatory
 microRNA ?

62. DNA
Information for all proteins stored in DNA
in the form of chromosomes or plasmids.
Chromosomes (both circular and linear)
consist of two strands of DNA wrapped
together in a left handed helix.
The strands of the helix are held together
by hydrogen bonds between the individual
bases. The “outside” of the helix consists of
sugar and phosphate groups, giving the DNA
molecule a negative charge.

63. Complimentary Base Pairs
A-T Base pairing G-C Base Pairing

64. DNA Structure
 The DNA helix is “anti-parallel”
 Each strand of the helix
has a 5’ (5 prime) end and
a 3’ (3 prime) end.

65. DNA Structure
Strand 1
(Watson strand)
Strand 2
(Crick strand)
5 ‘ end
3 ‘ end
3’ end
5’end

66. DNA Structure
 1 atgatgagtg gcacaggaaa cgtttcctcg atgctccaca gctatagcgc caacatacag
 61 cacaacgatg gctctccgga cttggattta ctagaatcag aattactgga tattgctctg
 121 ctcaactctg ggtcctctct gcaagaccct ggtttattga gtctgaacca agagaaaatg
 181 ataacagcag gtactactac accaggtaag gaagatgaag gggagctcag ggatgacatc
 241 gcatctttgc aaggattgct tgatcgacac gttcaatttg gcagaaagct acctctgagg
 301 acgccatacg cgaatccact ggattttatc aacattaacc cgcagtccct tccattgtct
 361 ctagaaatta ttgggttgcc gaaggtttct agggtggaaa ctcagatgaa gctgagtttt
 421 cggattagaa acgcacatgc aagaaaaaac ttctttattc atctgccctc tgattgtata
Because of the base pairing rules, if we know one
strand we also know what the other strand is.
Convention is to right from 5’ to 3’ with 5’ on the left.

67. Chromosomes and Plasmids
 Chromosomes are composed of DNA and
proteins.
 Proteins (histone & histone like proteins) serve a
structural role to compact the chromosome.
 Chromosomes can be circular, or linear.
 Both types contain an antiparallel double helix!
 Genes are regions within a chromosome.
 Like words within a sentence.
For an animation of the organization of a human chromosome see:
http://www.dnalc.org/ddnalc/resources/chr11a.html

68. RNA
 Almost all single stranded (exception is
RNAi).
 In some RNA molecules (tRNA) many of the
bases are modified (i.e. psudouridine).
 Has capacity for enzymatic function.
 One school of thought holds that early
organisms were based on RNA instead of
DNA (RNA world).

69. RNA
 Several different “types” which
reflect different functions
 mRNA (messenger RNA)
 tRNA (transfer RNA)
 rRNA (ribosomal RNA)
 snRNA (small nuclear RNA)
 RNAi (RNA interference)

70. RNA function
 mRNA – transfers information from DNA to
ribosome (site where proteins are made)
 tRNA – “decodes” genetic code in mRNA, inserts
correct A.A. in response to genetic code.
 rRNA-structural component of ribosome
 snRNA-involved in processing of mRNA
 RNAi-double stranded RNA, may be component of
antiviral defense mechanism.

71. RNA
A - hairpin loop
B- internal loop
C- bulge loop
D- multibranched loop
E- stem
F- pseudoknot
Complex secondary structures can form in linear molecule

72. mRNA
 Produced by RNA polymerase as product of transcription
 Provides a copy of gene sequence (ORF) for use in
translation (protein synthesis).
 Transcriptional regulation is major regulatory point
 Processing of RNA transcripts occurs in eukaryotes
 Splicing, capping, poly A addition
 In prokaryotes coupled transcription and translation can
occur