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BIOCHEMISTRY
PRELIMINARY
INTRODUCTION TO BIOCHEMISTRY
Biochemistry
- Chemistry of life
- Study of life processes, structures, mechanisms,
reactions at the molecular level
- Chemistry, Biology, & Genetics
Vitalism Theory
- Idea that substances and processes associated
with living organisms did not behave according
to the known laws of physics and chemistry
- Organic vs. Inorganic
Evidences for Vitalism
- Only living things have a high degree of
complexity
- Only living things extract, transform and utilize
energy from their environment
- Only living things are capable of self assembly
and self replication
Origins of Biochemistry: a challenge to vitalism and…
Famous Dead Scientists
1. Friedrich Wohler (19th century)
- Synthesized urea from inorganic
substance—ammonium cyanate.
2. Eduard Buchner and Hans Buchner (1897)
- found that glucose + dead yeast cells
are still able to undergo fermentation,
demonstrating that reactions can occur
in vitro.
3. Emil Fischer (1894)
- Each enzyme can only catalyze specific
complex molecules called substrates.
- proposed the lock and key theory, which
states that enzymes have a specific
shape that directly correlates to the
shape of the substrate.
4. James Batcheller Sumner
- studied the enzyme urease, which
breaks down urea into ammonia and
carbon dioxide
- An enzyme is protein
5. Gregor Mendel (mid-1900)
- Started describing genes.
- Father of Genetics
6. Oswald Avery, Colin McLeod, Maclyn
McCarty (1944)
- identified DNA as information molecules
7. James Watson (still alive) and Francis Crick
(1953)
- proposed the structure of the DNA
- In 1958 Crick proposed the central
dogma of biology
-
DNA -> RNA (mRNA) -> Protein
Replication -> Transcription -> Translation
Areas of Biochemistry
- Biomolecules. Structure and function of
biological macromolecules
- Metabolism
- Catabolism: Destructive phase
- Complex substance to subunits
(simpler substance)
- Anabolism: Constructive phase
- From simpler substance to
complex substance
- Molecular Genetics
- How life is replicated
- Regulation of protein synthesis
Objective of Biochemistry
- determine how the collections of inanimate
molecules that constitute living organisms
interact with each other to maintain and
perpetuate life
Scope of Biochemistry
- LIFE. chemistry of living matter in its different
phases of activity, from the smallest
microorganisms such as viruses to the most
complex ones as human
- Virus: has either DNA or RNA
- Cell: has both DNA and RNA
Chemical Reactions Occurring in Living Organism
Oxidation
- gains oxygen or loses hydrogen/electron
⇀ aerobic oxidation – takes place in the
presence of oxygen
⇀ anaerobic oxidation – occurs in the
absence of oxygen
Reduction
- gains hydrogen/electron or loses oxygen
Condensation
- Dehydration synthesis(union)
- Removal of water
Central Dogma
- Flow of information
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Hydrolysis
- Lysis = splitting
- Large molecules broken down
Cell Size
- Most cells are relatively small because as size
increases, volume increases much more rapidly.
- Cell size and shape are related cell functions.
A Scale of Visibility
Transfer Reactions
a. Phosphorylation - addition of phosphate group
b. Transamination - transfer of amino group
c. Acetylation - addition of acyl group
d. Transmethylation - transfer of methyl group
Decarboxylation
- Removal of carboxyl group
Uses of Biochemistry
The results of biochemical research are used extensively
in the world outside the laboratory
- Agriculture
- Pharmacology and Toxicology
- Medical Sciences
- Clinical Chemistry
- Nutrition
THE CELL AND ITS CHEMISTRY
Cells
-
Basic functional and structural unit of life
All living things are composed of cells, cell parts,
or cell products
- Organisms may be:
- Unicellular: prokaryotes
- Multicellular: human
Cell theory
- All organisms are composed of one or more
cells.
- Cells are the smallest living units of all living
organisms.
- Cells arise only by division of a previously
existing cell.
- Cells vary in size and shapes.
Cell Requirements
- Genetic material
- Single circular molecule of DNA in
prokaryotes
- Double helix located in nucleus in
eukaryotes
- Cytoplasm
- Fills cell interior (sugars, amino acids,
proteins, organelles)
- Plasma Membrane
- Encloses the cell
Classification of Cells
There are two major types of cells
- Prokaryotic
- lacks a nucleus and does not have an
extensive system of internal membranes
- all bacteria and archaea have this cell
type
- Eukaryotic
- has a nucleus and has internal
membrane-bounded compartments
- all organisms other than bacteria or
archaea have this cell type
Prokaryotic Cells
Prokaryotes are the simplest cellular organisms. They
have a plasma membrane surrounding a cytoplasm without
interior compartments (some bacteria have additional outer
layers to the plasma membrane)
Cell wall - comprised of carbohydrates to confer rigid
structure
Capsule may surround the cell wall
Cytoplasm is uniform with little or no internal support
framework
Ribosomes (sites for protein synthesis) are scattered
throughout the cytoplasm
Nucleoid region (an area of the cell where DNA is
localized)
not membrane-bounded, so not a true
nucleus
Flagellum (plural, flagellae) is a threadlike structure
made of protein fibers that extends from the cell
surface
may be one or many
aids in locomotion and feeding
Pilus (plural, pili) is a short flagellum
aids in attaching to substrates and in
exchanging genetic information between
cells
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The Plasma Membrane
The plasma membrane is conceptualized by the fluid
mosaic model–a sheet of lipids with embedded proteins. The
lipid layer forms the foundation of the membrane. The fat
molecules
comprising the lipid layers are called
phospholipids.
A phospholipid has a polar head and two non- polar
tails
The polar region contains a phosphate chemical
group and is water-soluble
The non-polar region is comprised of fatty acids and
is water-insoluble
Eukaryotic Cells
Eukaryotic cells are larger and more complex than
prokaryotic cells. They have a plasma membrane encasing the
cytoplasm, internal membranes form compartments called
organelles. The cytoplasm is semi-fluid and contains a
network of protein fibers that form a scaffold called a
cytoskeleton.
Nucleus - a membrane-bounded compartment for
DNA that gives eukaryotes (literally, “true-nut”) their
name
Endomembrane system - gives rise to the internal
membranes found in the cell. Each compartment can
provide specific conditions favoring a particular
process.
The cells of plants, fungi, and many protists have a
cell wall beyond the plasma membrane
All plants and many protists contain organelles called
chloroplasts
Plants contain a central vacuole
only animal cells contain centrioles
-
A lipid bilayer forms spontaneously whenever a
collection of phospholipids is placed in water
-
The interior of the lipid bilayer is completely nonpolar
no water-soluble molecules can freely cross
through it
cholesterol is also found in the interior
it affects the fluid nature of the
membrane
its accumulation in the walls of
blood vessels can cause plaques
plaques lead to cardiovascular
disease
Another major component of the membrane is a
collection of membrane proteins
some proteins form channels that span the
membrane
these are called transmembrane
proteins
other proteins are integrated into the
structure of the membrane
for example, cell surface proteins
are attached to the outer surface of
the membrane and act as markers
Proteins are embedded within the lipid bilayer
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The Nucleus: The Cell’s Control Center
The nucleus is the command and control center of the
cell
it also stores hereditary information
The nuclear surface is bounded by a doublemembrane called the nuclear envelope
groups of proteins form openings called
nuclear pores that permit proteins and RNA
to pass in and out of the nucleus
The DNA of eukaryotes is packaged into segments
and associated with protein
this complex is called a chromosome
the proteins enable the DNA to be
wound tightly and condense during
cell division
when the cell is not dividing, the
chromosomes exist as threadlike strands
called chromatin
protein synthesis occurs when the
DNA is in the chromatin form
The cell builds proteins on structures called
ribosomes
ribosomes consist of ribosomal RNA (rRNA)
and several different kinds of proteins
Ribosomes are assembled in a region of the nucleus
called the nucleolus
The Endomembrane System
The endoplasmic reticulum (ER) is an extensive
system of internal membranes
some of the membranes form channels and
interconnections
other portions become isolated spaces
enclosed by membranes
these spaces are known as
vesicles
The portion of the ER dedicated to protein synthesis
is called the rough ER
the surface of this region looks pebbly
the rough spots are due to embedded
ribosomes
The portion of the ER that aids in the manufacture of
carbohydrates and lipids is called the smooth ER
the surface of this region looks smooth
because embedded ribosomes are scarce
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After synthesis in the ER, the newly-made molecules
are passed to the Golgi bodies
Golgi bodies are flattened stacks of
membranes scattered through the cytoplasm
their numbers vary depending on the cell
their function is to collect, package, and
distribute molecules manufactured in the cell
the Golgi bodies of a cell are collectively
called the Golgi complex
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The ER and Golgi complex function together as a
transport system in the cell
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The Golgi complex also gives rise to lysosomes
these membrane-bound structures contain
enzymes that the cell uses to break down
macromolecules
worn-out cell parts are broken down
and their components recycled to
form new parts
particles that the cell has ingested
are also digested
Organelles That Harvest Energy
Eukaryotic cells contain energy harvesting organelles
that contain their own DNA
these organelles appear to have been
derived from ancient bacteria that were
taken up by eukaryotic cells
these organelles include mitochondria and
chloroplasts
Mitochondria are cellular powerhouses
Sites for chemical reactions called oxidative
metabolism
The organelle is surrounded by two membranes
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Chloroplasts are the sites of photosynthesis
The organelle is also surrounded by two membranes
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Both mitochondria and chloroplasts possess their own
molecule of circular DNA
They cannot be grown free of the cell
they are totally dependent on the cells within
which they occur
The theory of endosymbiosis
states that some organelles evolved from a
symbiosis in which one cell of a prokaryotic
species was engulfed by and lived inside of
a cell of another species of prokaryote that
was a precursor to eukaryotes
the engulfed species provided their hosts
with advantages because of special
metabolic activities
the modern organelles of mitochondria and
chloroplasts are believed to be found in the
eukaryotic
descendants
of
these
endosymbiotic prokaryotes
-
-
In addition to the double membranes and circular
DNA found in mitochondria and chloroplasts, there is
a lot of other evidence supporting endosymbiotic
theory
mitochondria are about the same size as
modern bacteria
the cristae in mitochondria resemble folded
membranes in modern bacteria
mitochondrial ribosomes are similar to
modern bacterial ribosomes in size and
structure
mitochondria divide by fission, just like
modern bacteria
The Cytoskeleton and Related Structures
The cytoskeleton is comprised of an internal
framework of protein fibers that
anchors organelles to fixed locations
supports the shape of the cell
helps organize ribosomes and enzymes
needed for synthesis activities
The cytoskeleton is dynamic and its components are
continually being rearranged
Three different types of protein fibers comprise the
cytoskeleton
Intermediate filaments
thick ropes of intertwined protein
Microtubules
hollow tubes made up of the protein
tubulin
Microfilaments
long, slender microfilaments made
up of the protein actin
The protein fibers of the cytoskeleton
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Centrioles are complex structures that assemble
microtubules in animal cells and the cells of most
protists
they occur in pairs
they are found near the nuclear envelope
they are composed of microtubules
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Cellular motion is associated with the movement of
actin microfilaments and/or microtubules
some cells “crawl” by coordinating the
rearrangement of actin microfilaments
some cells swim by coordinating the beating
of microtubules grouped together to form
flagella or cilia
Cilia and Flagella are hairlike structures projecting
from the cell that function to move the cell by their
movements
Cilium (Cilia) - the short, numerous
appendages
Flagellum (Flagella) – the longer, less
numerous appendages
Eukaryotic Cell Surfaces and Junctions
Cells interact with their environments and with each
other via their surfaces.
Plant cells are supported by rigid cell walls made
largely of cellulose.
Plant cells connected by plasmodesmata.
Animal cells are embedded in an extracellular matrix
consisting mainly of glycoprotein. This matrix is
responsible for binding cells together in tissues.
-
Manufacture
Nucleus, ribosomes, RER, SER, Golgi
complex
Breakdown
Lysosomes, peroxisomes, vacuoles
Energy Processing
Chloroplasts, mitochondria
Support, Movement and Communication Between
Cells
Cytoskeleton, cell walls, extracellular matrix,
junctions
Transport of Materials
Passive Transport: does not require energy. Moves
along concentration gradient
Diffusion
Osmosis
Facilitated Diffusion
Active Transport: requires energy.
Endocytosis
Exocytosis
Diffusion and Osmosis
Movement of water and nutrients into a cell or
elimination of wastes out of cell is essential for
survival
This movement occurs across a biological membrane
in one of three ways
diffusion
membrane folding
transport through membrane proteins
Molecules move in a random fashion but there is a
tendency to produce uniform mixtures
The net movement of molecules from an area of
higher concentration to an area of lower concentration
is termed diffusion
Molecules diffuse down a concentration gradient from
higher to lower concentrations
diffusion ends when equilibrium is reached
Diffusion
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The concentration of all molecules dissolved in a
solution is called the osmotic concentration of the
solution
if the osmotic concentrations of two solutions
is equal, the solutions are each called
isotonic
if two solutions have unequal osmotic
concentration, the solution with the higher
solute concentration is said to be
hypertonic, and the solution with the lower
solute concentration is said to be hypotonic
Movement of water by osmosis into a cell causes
pressure called osmotic pressure
enough pressure may cause a cell to swell
and burst
osmotic pressure explains why so many cell
types are reinforced by cell walls
Osmotic pressure in plants and animal cells
**Osmos means to push
Forms of Endocytosis
Phagocytosis is endocytosis of particulate (solid)
matter. “eat”
Pinocytosis is endocytosis of liquid matter. “drink”
Exocytosis
Chemistry of Life
Inorganic Compounds
Water
Gases
Minerals
Organic Compounds
Carbohydrates
Proteins
Lipids
Nucleic acids
Vitamins
Hydrogen Bonds Give Water Unique Properties
Water is essential for life
the chemistry of life is water chemistr
Water is a polar molecule
water can form hydrogen bonds
hydrogen bonding confers on water many
different special properties
Heat Storage
water temperature changes slowly and holds
temperature well
Ice Formation
few hydrogen bonds break at low
temperatures
water becomes less dense as it
freezes because hydrogen bonds
stabilize and hold water molecules
farther apart
High Heat of Vaporization
water requires tremendous energy to
vaporize because of all the hydrogen bonds
that must be broken
when water vaporizes, it takes this heat
energy with it, allowing for evaporative
cooling
Ice formation
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Water molecules are attracted to other polar
Molecules
cohesion – when one water molecule is
attracted to another water molecule
adhesion – when polar molecules other than
water stick to a water molecule
High polarity
in solution, water molecules tend to form the
maximum number of hydrogen bonds
hydrophilic molecules are attracted
to water and dissolve easily in it
these molecules are also
polar
and can form
hydrogen bonds
hydrophobic molecules are repelled
by water and do not dissolve
these
molecules
are
nonpolar and do not form
hydrogen bonds
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Pure water has a pH of 7
there are equal amounts of [H+] relative to
[OH-]
Acid – any substance that dissociates in water
and increases the [H+]
acidic solutions have pH values below 7
Base – any substance that combines with [H+] when
dissolved in water
basic solutions have pH values above 7
The pH in most living cells and their environments is
fairly close to 7 (6.9–7.3)
proteins involved in metabolism are sensitive
to any pH changes
Organisms use buffers to minimize pH disturbances
a buffer is a chemical substance that takes
up or releases hydrogen ions
Organic compounds
Biomolecules - associated with living things. Organic
molecules
Carbohydrates – major source of energy (a.k.a.
sugars)
Proteins – for tissue repair
Lipids – constituents of membranes, also a source of
energy (a.k.a. Oils and fats)
Nucleic Acids – genetic material and for protein
synthesis
CARBOHYDRATES
Water Ionizes
The covalent bond within a
sometimes breaks spontaneously
water
molecule
H2O ↔ OH- + H+
-
This produces a positively hydrogen ion (H+) and a
negatively charged hydroxide ion (OH-)
The amount of ionized hydrogen from water in a
solution can be measured as pH
The pH scale is logarithmic, which means that a pH
scale difference of 1 unit actually represents a 10-fold
change in hydrogen ion concentration
Carbohydrates
provide energy through oxidation
serve as a form of stored chemical energy
supply carbon for the synthesis of cell components
form part of the structures of some cells and tissues
a molecule that contains the elements CHO in a 1:2:1
ratio
sizes vary (simple and complex carbohydrates)
building block is simple sugar or monosaccharide
Carbohydrates or saccharides (saccharon) are
polyhydroxy aldehydes or ketones, or substances that
yield such compounds on hydrolysis
An aldehyde is an organic compound in
which the carbonyl group is attached to a
carbon atom at the end of a carbon chain. A
ketone is an organic compound in which the
carbonyl group is attached to a carbon atom
within the carbon chain.
Stereochemistry of Carbohydrates
Two Forms of Glyceraldehyde (enantiomers)—not
the same as each other; one enantiomer cannot be
superimposed on the other. Enantiomers are mirror
images of each other.
D-glyceraldehyde
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L-glyceraldchyde
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Chiral Carbons
any carbon atom which is connected to four different
groups will be CHIRAL, and will have two
nonsuperimposable mirror images (The mirror images
are called enantiomers)
An achiral object is identical with (superimposable on)
its mirror image.
-
2 raised to n Rule
when a molecule has more than one chiral carbon,
each carbon can possibly be arranged in either the
right-hand or left-hand form, thus if there are n chiral
carbons, there are 2n possible stereoisomers
Fischer Projection
are a convenient way to represent mirror images in
two dimensions
Place the carbonyl group at or near the top and the
last achiral carbon at the bottom
Naming Stereoisomers
look at the chiral carbon farthest from the carbonyl
group:
if the hydroxyl group points to right when the
carbonyl is up, it is the D-isomer
if the hydroxyl group points to left when the
carbonyl is up, it is the L-isomer
The presence of an aldehyde is indicated by
the prefix aldo- and an ketone by the prefix
ketoProperties
of
Monosaccharides
(Carbohydrates)
monosaccharides & disaccharides
are white crystalline substance;
starches are amorphous powder;
cellulose is fibrous
solubility to ordinary solvents is
inversely
proportional
to the
complexity of their structures
monosaccharides & disaccharides
are sweet; starch and cellulose are
tasteless
Reducing power - the potential or
power of any substance to reduce
another substance. Substance is
able to donate electrons.
Fermentation - Sugar undergoing
fermentation (with yeast) produces
ethyl alcohol and carbon dioxide
Osazone formation - The reaction
(oxidation) between three moles of
phenylhydrazine and one mole of
aldose produces a crystalline
product known as phenylosazone
Action of alkalis - Strong alkalies,
like strong acids, decompose the
sugars. This process identifies the
reducing property of sugar
Action of acids - acid-catalyzed
aldolized glycosides hydrolyzed
back to alcohol & sugar
Oxidation
Oxidized
to
carboxyl/COOH
Chiral Carbon Atoms
-
Classes of Carbohydrates
A. Monosaccharides
simplest of the carbohydrates,since they
contain only one polyhydroxy aldehyde or
ketone
Monosaccharides are classified according to
the number of carbon atoms they contain:
3 carbon atoms - triose
4 carbon atoms - tetrose
5 carbon atoms - pentose
6 carbon atoms - hexose
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Reduction - Reduced to sugar
alcohol
monosaccharides do not usually
exist
in
solution
in
their
"open-chain" forms
an alcohol group can add into the
carbonyl group in the same
molecule to form a pyranose ring
containing a stable hemiacetal
(aldehyde) or hemiketal (ketone)
Haworth projection is a common way of
writing a structural formula of sugars
(monosaccharides and disaccharides) with
an
unpretentious
three-dimensional
perspective. Pyranose Ring (piattos)
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B.
C.
Formation of Phosphate Esters
Phosphate Esters
a
class
of
organophosphorus
compounds
with
the
general structure O=P(OR)
3, a central phosphate
molecule with alkyl or
aromatic substituents.
phosphate esters can form
at
the
6-carbon
of
aldohexose
and
ketohexose
sugar-phosphate
backbone of DNA & RNA,
ATP
Monosaccharide derivatives
Deoxy sugars
Sugars that have had
hydroxyl group replaced
with hydrogen atom
Amino sugars
Sugars where hydroxyl
group is replaced with an
amino group
Alcohol sugars
Polyhydric
alcohols
(polyols) formed when the
carbonyl group of the
monosaccharide
is
reduced to hydroxyl group
(one -OH/hydroxyl group
attached to each carbon)
Carboxylic Acid sugars
A carbonyl or hydroxyl
group is oxidized to a
carboxylic acid group
Common Monosaccharides
Glucose
Fructose
Galactose
Oligosaccharides
Contain 2-10 monosaccharide units
Disaccharides
Two monosaccharides linked together
through a glycosidic linkage
D.
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Common Disaccharides
Sucrose
table sugar
glucose + fructose
Lactose
found in mammary milk
glucose + galactose
Maltose
found in molasse
used to ferment beer
glucose + glucose
Polysaccharides
Contains hundreds/thousands carbohydrate
units
Not reducing sugar
Two types:
Homopolysaccharides - one type of
monosaccharides
Heteropolysaccharides - multiple
types of monosaccharides
Starch
polymer consisting of glucose units
insoluble in water because of high
molecular weight
forms of starch:
1. Amylose
unbranched
chains connected
by
(1-4)
glycosidic
linkages
10-20% in plants
amylose chain is
flexible enough to
allow
the
molecules to twist
into shape of a
helix
2. Amylopectin
consists of long
chains of glucose
connected
by
(1-4)
glycosidic
linkages,
with
(1-6)
branches
every 24 to 30
glucose
units
along the chain
80-90% of the
starch in plants is
in this form
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Glycogen
aka animal starch
structurally similar to amylopectin,
containing both (1-4) and (1-6)
glycosidic linkages
abundant in the liver and muscles
on hydrolysis, it forms glucose
Cellulose
polymer
consisting
of
long,
unbranched chains of glucose
connected by (1-4) glycosidic
linkages
most
important
structural
polysaccharide;
single
most
abundant organic compound on
earth
dietary fiber
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AMINO ACIDS AND PROTEINS
Proteins
are complex macromolecules that are polymers of
many subunits called amino acids
roles in living things
catalysts-enzymes
hormones
transport molecules
key part of structures
muscle action
immune response
visual process
operation of the nervous system
Proteins come in all shapes and sizes
Functional group gives amino acids their
chemical identity
Basic Structure of an Amino Acid
Things to remember about amino acids:
only 20 L-amino acids are used to make
proteins; AA are joined by peptide bonds
side chains or side groups are what
distinguish amino acids from each other
amino acids can exist as zwitterions (a
molecule or ion having separate positively
and negatively charged groups)
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Amino Acids
these are small molecules with a simple basic
structure, a carbon atom to which three groups are
added
amino group (-NH2)
carboxyl group (-COOH)
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Writing AA starts from
C-terminus
Classification of Amino Acids:
I.
Polarity
polar
acidic
basic
neutral
nonpolar
II.
R group
acidic
basic
neutral
III.
Nutrition
essential
non-essential
N-terminus
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Polypeptide
Count the amino acid residue
To find the peptide bond locate the carbonyl
Proteins structure
protein structure is complex
the order of the amino acids that form the
polypeptide affects how the protein folds
together
the way that a polypeptide folds to form the
protein determines the protein's function
some proteins are comprised of
more than one polypeptide
Primary Protein Structure
Sequence of a chain of amino acids
-
Secondary Protein Structure
Local folding of the polypeptide chain into
helices or sheets
-
Tertiary Protein Structure
Three-dimensional folding pattern
protein due to side chain interactions
Proteins
the covalent bond linking two amino acids together is
called a peptide bond
the assembled polymer is called polypeptide
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Quaternary Protein Structure
protein consisting of more than one amino
acid chain
Properties of proteins
very large molecules
have characteristic amino acid composition
some proteins contain prosthetic group
generally tasteless, mostly colorless
insoluble in non-polar solvents; varied degrees of
solubility in water, salt solution, dilute acids and bases
Amphoteric - able to react both as a base and as an
acid
very reactive and highly specific
Classifications of proteins
I.
According to structure
simple proteins
compound proteins
II.
According to shape
globular
fibrous
III.
According to function
contractile
defense
enzymes
regulatory
storage
structural
transport
Enzymes Parts
Apoenzyme
enzymatically inactive protein part of an
enzyme, which requires a cofactor for its
activity
Cofactor
a non-protein chemical compound or metallic
ion that is required for an enzyme's role as a
catalyst
Proenzyme or zymogen
a biologically inactive substance which is
metabolized into an enzyme.
Coenzyme
organic compounds required by many
enzymes for catalytic activity
Enzymes Nomenclature
Trivial System
based on the substrate of the enzyme and
the type of reaction catalyzed
use of -ase ending
International Enzyme Commission
groups enzymes into six classes
Main Classes of Enzymes
Proteins Denaturation
changes to the environment of the protein may cause
it to unfold or denature
increased temperature or lower pH affects hydrogen
bonding, which is involved in the folding process
a denatured protein is inactive
Properties of Enzymes
enzymes are proteins
enzymes are catalysts
enzymes are highly specific
Chemical Reactions
All chemical reactions require an initial input of energy
called activation energy
reactions become more likely to happen if their
activation energy is lowered
this process is called catalysis
catalyzed reactions proceed must faster than
non-catalyzed reactions
ENZYMES
Main Classes of Enzymes
What are enzymes?
Catalysts
substances that speed up chemical reactions
enzymes are specific for one particular reaction or
group of related reactions
many reactions cannot occur without the correct
enzyme present
General Characteristics of Enzymes
Enzymes are well-suited to their roles in three major ways:
they have enormous catalytic power
they are highly specific
their activity can be regulated
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How Enzymes Work
enzymes bind specifically to a molecule and stress
the bonds to make the reaction more likely to proceed
active site is the site on the enzyme that binds to a
reactant
binding site is the site on the reactant where the
enzyme binds
the binding of the reactant to an enzyme causes the
enzyme's shape to change slightly - leading to an
"induced fit"
the enzyme lowers the activation energy for the
reaction
the enzyme is unaffected by the chemical reaction
and can be reused
Mechanism of Enzyme Action
Lock and Key Theory
enzymes have a specific shape that directly
correlates to the shape of the substrate.
Induced Fit Theory
an enzyme's shape and conformation
changing over time in response to substrate
binding.
How cells regulate enzymes?
Cells can control enzymes by altering their shape
Repressors
feedback inhibition
Activators
Enzyme Inhibition
a decrease in enzyme-related processes, enzyme
production, or enzyme activity.
How Enzymes Work
Temperature and pH affect enzyme activity
enzymes function within an optimum
temperature range
enzymes function within an optimal pH range
IGANO, CIENNA CHARRISE
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