BI 149 Cellular & Molecular Biology 1

BIOLOGICAL MOLECULES  most are ring-form  glycosidic bonds:

(the building block when a C1 of one
form) sugar reacts with
I. CARBOHYDRATES linking sugars
 linear forms are the hydroxyl group
shape
monomer sugars significant in of another sugar
aka “glycans” medicine – aldehyde  -C-O-C- linkage
groups are very
 chemical energy
reactive

monosaccharides
stores (short-term)
 a Carbon atom
 durable building  simple sugars
functions & bonded to four
materials for  examples: glucose,
features different groups
biological fructose, galactose
can have 2 possible
construction
configurations
 polar
 mirror images that
(CH2O)n
general formula *sugars of importance
cannot be  molecules composed of 2
are n=3 to 7 superimposed on sugar units
stereoisomerism each other
 3, trioses  readily available
 same chemical

classified by number of monomers

disaccharides
 4, tetroses energy stores
reactivities  examples:
carbon atoms  5, pentoses
 direction of o sucrose (glucose +
 6, hexoses
projection fructose)
 7, heptoses o D-[sugar]: right o lactose (glucose +
backbone of carbon o L-[sugar]: left galactose)
atoms *typically, the D-sugars o maltose (glucose +
 single bonded are used in cells
glucose)
 linear array the carbon associated
C1 atom  short chains of sugars
with the aldehyde

oligosacchari
structure  each linked to a linked together
hydroxyl group (-  the aldehyde/ketone
 often covalently linked

des
OH) tends to react with
a hydroxyl of the to lipids (glycolipids)
 except one linked and proteins
same
to a carbonyl group (glycoproteins)
molecule, making a
(-CO-)
ring (C1 joins with  a polymer of sugar
 internal – ketone
C5) units joined by

polysaccharides
 at an end – self-reaction
carbonyl group  straight chain > glycosidic bonds
aldehyde*
*bonded to at least 1
pyranose  examples:
hydrogen atom  OH projections o nutritional – starch,
o -pyranose: glycogen
below o structural – chitin,
o -pyranose: cellulose,
upward glycosaminoglycans

BIOLOGICAL MOLECULES
BI 149 Cellular & Molecular Biology 2

 cis (Z) configuration  carry out virtually

II. LIPIDS o produces kinks in the all of a cell’s
chain activities
building functions &  virtually unlimited
fatty acids o naturally occurring
block
fatty acids are in this features molecular structures
 nonpolar configuration  high degree of
general  ability to dissolve in configuration  trans (E) configuration specificity
functions & organic solvents  polar
features  inability to dissolve in
AMINO ACIDS
water
FATS  carboxyl group (—
COOH)
 very rich in chemical
energy components  amino group
functions &  separated by an α-
 long-term energy storage  chemically reducing
features carbon
 stored in cells in liquid double bonds with
droplets hydrogen atoms  α-carboxyl group
hydrogenation
 converts some of the cis loses a p+ and exists
 a glycerol molecule
double bonds into trans in a negatively
 linked by ester bonds double bonds (straight) in a neutral charged state (—COOH-
components
 to 3 fatty acids STEROIDS aqueous )
(“triglyceride”) solution...  α-amino group accepts
functions &  4-ringed hydrocarbon
 long unbranched a p+ and exists in a
features skeleton
hydrocarbon chains positively charged
PHOSPHOLIPIDS state (NH3+)
(hydrophobic tail)
fatty acids  a small polar group  D-form
 single carboxyl group at
one end (-COOH)  covalently linked to a (microorganisms)
two forms of
(hydrophilic head) polar phosphate group  L-form (synthesis of
amino acids
 in turn covalently protein on a
 differ in length of
linked to a glycerol ribosome)
hydrocarbon chain
backbone incorporated
 typically 14 to 20 components
 linked by ester bonds to into a
carbon atoms amino acid > “residue”
2 fatty acid chains polypeptide
 presence/absence of chain
variations double bonds
POLYPEPTIDE CHAINS
o saturated – lacking
double bonds, solid at
room temperature  long, continuous,
o desaturated – having unbranched polymer
double bonds, liquid III. PROTEINS features  made of amino acids
at room temperature joined by peptide
monomer amino acids bonds

BIOLOGICAL MOLECULES
BI 149 Cellular & Molecular Biology 3

 average contains 450 participate in  has its α-amino

amino acids chemical reactions group as part of a
 form H-bonds Tyr ring
 associate with  has hydrophobic
water Pro character
 hydrophobic side Ala  can create kinks in
chain consists polypeptide chains
 condensation of two almost entirely of Val  can disrupt ordered
amino acids C and H atoms secondary structure
Leu
 when each amino acid (lacking O and N, amino acids found in

nonpolar
formation becomes joined to two generally) Ile proteins that arise by
posttranslation
other amino acids [on  tend to form inner alterations to the R
al
either side] core of soluble Met group post-
modifications
 elimination of H2O proteins (away from incorporation into the
aqueous medium) Phe polypeptide chain
 associate with PROTEIN STRUCTURE
 N-terminus: amino Trp
lipid bilayer
acid with a free α-  specific linear
ends of the amino group  can fit into either
sequence of amino
hydrophobic or
chain  C-terminus: amino acids that constitute
hydrophilic
acid with a free α- the chain
environment
carboxyl group Gly  the number of
 often resides at primary
special side chains different
 hydrophilic side sites where two
Asp polypeptides that can
chains act as polypeptides come
be formed = 20n, (n =
acids/bases into close contact
Glu amino acids in the
polar, charged

 tend to be fully  contains a reactive chain)

charged (+/-) sulfhydryl (—SH)
side chain properties

Lys  conformation (3D

under  has polar,
uncharged character arrangement) of
physiological
Arg Cys portions of the
conditions  can form a covalent

secondary
polypeptide chain
 form ionic bonds bond with another
cysteine to form a  polypeptide chains
 often involved in His definition
exist in preferred
chemical reactions disulfide link conformations that
Ser provide maximum
 hydrophilic side possible # of bonds
uncharged

chains tend to
polar,

Thr between neighboring

have partial amino acids
charges (+/-) Gln
allowing them to Asn

BIOLOGICAL MOLECULES
BI 149 Cellular & Molecular Biology 4

 backbone inside the  determines the  secondary –

helix interactions and structural and
 side chains enzymatic activity of catalytic
α helix projecting outward a protein  deoxyribose nucleic
cylindrical  stabilized by  domains: 2 or more acid (DNA): genetic
twisting hydrogen bonds spatially distinct material of all
spiral between atoms of modules that fold cellular organisms
peptide bond above independently of one  ribose nucleic acid
and below it along another types
(RNA): genetic
the spiral  subunit: complexes of material of most
 backbone assumes a more than one chain viruses
folded/pleated o covalent disulfide STORED INFO IN DNA >
bonds FORM RNA MESSAGES >
conformation
GOVERN CELLULAR ACTIVITY
 hydrogen bonds o [more common]
noncovalent bonds  5-Carbon Sugar
 pleated oriented
via hydrophobic (ribose) <linked to
sheets perpendicular to quaternary
patches 1’ C of sugar>
several the long axis of
 protein complexes  nitrogenous base
segments of the chain, project
o homodimer: identical o purines (smaller,
a across
subunits single ring)—Adenine
polypeptide  strands can be
side by side o heterodimer: and Guanine
parallel or components
nonidentical o pyrimidines (larger,
antiparallel
subunits double ring)—
 highly extended, Cytosine and Uracil,
resists tensile PROTEIN FOLDING [in DNA Thymine]
forces unfolding or  phosphate group
 hinges, turns, disorganization of a <linked to 5’ C of
loops, or finger- denaturation protein; can be sugar>
like extensions achieved by a variety
others  RNA is a continuous
 often most flexible of reducing agents
single strand
 greatest protein in correctly
bioactivity
native state  may fold back on
folded form
itself to produce
 entire conformation features
o double-stranded
of the polypeptide
IV. NUCLEIC ACIDS segments
 not fixed for all
o three-dimensional
proteins monomer nucleotide structures
tertiary  categories  primary – storage and
o fibrous (structural, functions transmission of
exterior) genetic information
o globular (within the
cell)

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BI 149 Cellular & Molecular Biology 5

 do not carry genetic

information
 function as
structural scaffolds
where proteins can be
ribosomal RNA attached
 recognize and bind
soluble components
for protein synthesis
 “ribozymes”: RNA
enzymes

 ATP
other  GTP: Guanine
nucleotides triphosphate
o binds to G proteins
o switch on activity

BIOLOGICAL MOLECULES