LARGE BIOLOGICAL MOLECULESChapter 5
FUEL FOR LIVING SYSTEMS Large molecules are important for the basic
processes of life Grouped into 4 classes of organic compounds
Carbohydrates* Lipids Proteins* Nucleic acids*
Important to know how these are made, stored, and destroyed
Also, structure and function
* are considered macromolecules
POLYMERS
Chain of similar repeating units linked by covalent bonds E.g CAT-CAT-CAT-CAT=CAT-CAT or the alphabet Carbs, proteins, and nucleic acids are examples
The similar repeating units are called monomers E.g CAT or any letter of alphabet Joined and broken by reversible reactions
Enzymes can speed the reaction E.g digestion: cells need organic molecules broken
down so can be absorbed after which they can be rebuilt
POLYMERS
Dehydration reaction Links monomers Loss of water for each
monomer added Forms a covalent bond
Hydrolysis reaction Breaks polymers Addition of water for
each broken bond
Making polymers Breaking polymers
1 42
21
3
3 4
1
2
2 3
3
4
41
EXAMPLES OF POLYMERS
Small molecules are ordered to dictate life DNA is a polymer composed of 4 monomers
(nucleiotides) Creates variation based on arrangement
Proteins are polymers from 20 different amino acids (AA’s)
Sequence variation separates humans from flowers and individuals from individuals
CARBOHYDRATES
Simple sugars and polymers of simple sugars Sugars are broken down based on the number of
polymers Monosaccharides Disaccharides Polysaccharides
Each is joined by a dehydration reaction Polymers of sugar are actually what is
generally considered a carbohydrate or starchy food
MONOSACCHARIDES
Glucose is most common Major nutrient for cells Respiration, fuel for cellular work, and raw
material Trademarks of sugars
Molecular repeating unit of CH2O- Carbonyl and hydroxyl functional groups 3-7 carbons long
Hexoses (6 carbons, e.g glucose and fructose) Pentoses (5 carbons, e.g ribose and dioxyribose)
End in “-ose”
GLUCOSE VS FRUCTOSE
Also are examples of what?
DISACCHARIDES 2 monosaccharides
joined by a covalent bond Result of dehydration
reaction Form a glycosidic
bond/linkage Maltose
glucose + glucose Whoppers, malts, beer
Sucrose Glucose + fructose Table sugar Plant sap
Lactose galactose + glucose
POLYSACCHARIDES
Multiple glycosidic linkages Storage material until needed
Hydrolysis will break apart to provide sugars to cells
Building materials for cell protections 4 types
Starch Glycogen Cellulose Chitin
POLYSACCHARIDES FOR STORAGE
Starch Polymer of many glucose monomers Plants use as storage
Form of plastids Stockpiled glucose = stored E
E.g potatoes, grains, wheat, and corn Glycogen
More branched polymer of glucose Vertebrate storage in liver and muscles
Hydrolyzed when sugar is needed Not good for long term because depleted quickly
CELLULOSE
Cell wall of plant cells Most abundant organic compound on Earth Polymer of glucose with different linkages Straight molecule, grouped to form microfibrils
= strong Major component of paper and only of cotton
Most animals can’t hydrolyze Undigested, stimulates GI tract through abrasion
to stimulate mucous secretion Most fresh fruits, vegetables, and whole grains
Insoluble fiber on packages
CHITIN Composes arthropod exoskeletons
CaCO3 covers body and hardens Molted off and commonly eaten as Ca2+ source
Cell walls in fungi Used for surgical thread
Dissolvable stitches
LIPIDS ‘Grab bag’ of molecules
Not true polymers Not really big enough to
be macromolecules All mix poorly with
water due to hydrophobic nature (hydrocarbon chains)
Form ester linkages 3 types
Fats Phospholipids Steroids
FATS Glycerol (alcohol w/ 3 carbons) and fatty acids (16-
18 carbons and carboxyl end) Hydroxyl and carboxyl linkage = ester linkage
(triglyceride) Can be saturated or unsaturated Hydrogenated vegetable oils
Unsaturated synthetically to saturated by adding hydrogens Peanut butter and margarine to prevent separation Trans fats when conversion changes conformation of double
bond
Necessary for energy storage (hydrogen bonds) More compact, better for mobility Adipose storage
Cushions vital organs and insulates
SA
TU
RA
TED
VER
SU
S
UN
SA
TU
RA
TED
CH
AIN
S
Saturated
All single bonds with H
Most animal fats Solid, close
bonds; e.g butter
Unsaturated
Carbon carbon double bonds
Most plant and fish fats
Liquid, can’t bind close = bend; e.g olive oil
PHOSPHOLIPIDS
Makes up cell membranes Glycerol with 2 FA’s and 1
phosphate (negative charge) Hydrocarbons make
hydrophobic (form tails) Phosphate and attachment
are hydrophilic (form heads)
Bi-layered to protect hydrophobic from water
STEROIDS
Lipids with 4 fused rings Synthesized from cholesterol, common in
animal cell membranes Precursor to sex hormones Synthetic variants
Anabolic steroids (Testosterone)
PROTEINS
Necessary for almost anything living organisms do
Know types and functions from table 5.1 Enzymes regulate metabolism by acting as
catalysts Speed reactions w/o being consumed
Unique 3D shapes Formed from polypeptides (polymers of
amino acids) 20 AA’s, same set for all Protein = 1+ polypeptide folded and coiled into
specific 3D shape
AMINO ACID MONOMERS Common structure
Carboxyl and amino group
α-carbon is middle with H and R group (variable) Determines specific AA
from fig. 5.17
Side chains grouped by properties Nonpolar, hydrophobic Polar, hydrophilic Acidic, (-) charge b/c
carboxyl group Basic, (+) charge b/c
amino group Charges = hydrophilic
Polymers formed by peptide bonds
STRUCTURE AND FUNCTION
Polypeptides ≠ protein AA sequence does 4 levels of structure
1°-seq of AA, determined by genes 2°-repeated coils or folds for overall shape
H-bonds b/w carboxyl and amino backbone α-helix = H bonds b/w 4th AA ß-pleated sheet = 2+ regions of H bonds
3 °- interactions b/w side chains Hydrophobic interaction = side chains cluster in Disulfide bridges = -SH side chain interactions
4°-overall structure of 2+ polypeptides
PROTEIN STRUCTURE AND FUNCTION Polypeptides ≠
protein 1°: genes decide 2°: H-bonds b/w
carboxyl and amino
α-helix: 4th AA Β-sheet: 2+
regions of side by side H-bonds
3°: hydrophobic side chains and disulfide bridges
4 : 2+ polypeptides
CHANGING PROTEIN STRUCTURE
Sickle cell Single AA substitution in hemoglobin
Abnormal shape RBC’s that clogs vessels
Denaturation Proteins unravel and lose shape pH, [salt], temp, and other effects can cause Inactivates proteins
Removing agents might reverse
Misfolding Accumulate and cause detrimental problems E.g Alzheimer’s and Parkinson’s disease
Often times unfolding exposes hydrophobic areas to the aqueous solutions surrounding the protein
Aggregates to protect itself
PR
OTEIN
MIS
FO
LD
ING
NUCLEIC ACIDS Polymers of nucleotides (polynucleotides)
Blueprint for proteins to control all of cellular workings
Control of reproduction DNA RNA proteins
Central dogma of molecular biology Occurs in ribosomes
Monomer is a nucleotide Structure consists of 3 components
Nitrogenous base 5 carbon sugar Phosphate group
NUCLEOTIDE
Nitrogenous base Pyrimidine = a 6 member carbon and nitrogen
ring cytosine (C), thymine (T), uracil (U)
Purines = 6 member carbon ring fused to a 5 member ring (smaller name, bigger structure) adenine (A) and guanine (G)
DNA – C, T, G, and A RNA – C, U, G, and A
5 Carbon sugar Ribose Deoxyribose (missing oxygen)
NUCLEOTIDE POLYMERS
Phosphodiester linkage = phosphate joins sugars of 2 nucleotides For backbone of DNA Phosphate on 5’ carbon joins hydroxyl on 3’
carbon DNA codes 5’ -3’ Sequence of bases unique to each gene
Linear order of nitrogenous bases in a gene specifies AA sequence (which level of structure ?) Start codon
ATG and AUG = DNA and RNA Stop codon
UAG, UAA, UGA
DOUBLE HELIX
1st proposed by Watson and Crick Sugar-phosphate
backbones are antiparallel
Nitrogenous bases face in and H-bonds hold them together
2 strands are complementary
Binding specific A binds w/ T G binds w/ C