PROTEINS

PROPERTIES. TYPES OF
PROTEINS
LECTURE 8
 Protein properties

1. Molecular weight
• varies between 5000 and 4200000 Da.
• can be determined by different methods:
a) Chemical methods of sequencing of the component amino acids. Knowing the number and the type of
amino acids, molecular weight of the protein can be exactly calculated.
b) Ultracentrifugation. The sedimenting constant, S, is determined

dx / dt
S =
w2 *x
Molecular weight
RTS
=
D (1 - V x d)
c) Gel filtration chromatography
d) Determination of osmotic pressure

• Molecular weight of proteins is used

for their separation by dialysis.
Proteins, having high molecular
weight, cannot pass through a semi
permeable membrane and remain in
solution; the compounds with low
molecular weight can pass through the
membrane, being separated of
proteins.
• This principle is applied in therapy -
blood dialysis of patients with renal
failure; the catabolic products – urea,
uric acid, etc – are removed from
blood.
f) SDS-PAGE elecrophoresis
e) MALDI-TOFF mass spectrometry
2. Solubility

• Proteins have, generally, a high molecular weight ⇒ cannot form solutions

but colloid solution
• Colloidal solutions of proteins exert an osmotic pressure toward semi
permeable membranes. This property is essential for plasma proteins
which so regulate the changing of substances at the level of blood vessels.
• Diminishing of plasma protein quantity produces the entering of water into
tissues, phenomenon known as oedema.
• solubility depends on the protein conformation.
• ⇒ most fibrous proteins are insoluble in water.
• ⇒ globular proteins - solubility depends on the orientation of hydrophobic
amino acids.
• membrane proteins - hydrophobic amino acids are oriented toward
exterior, these proteins being water insoluble.
• cytoplasm globular protein - the orientation of the hydrophobic residues is
toward interior, these proteins being water soluble.
• Water solubility depends on:
a) salt concentration of the solution:
• At low concentrations, 1-10%, solubility is higher.
• At high concentrations, proteins cannot form bonds with water and
aggregate between them, precipitating.
b) Organic solvents, as ethanol, acetone, have similar competing effects
as protein molecule for water.
• ⇒ high concentrations of salts (sodium sulphate, ammonium sulphate,
etc), alcohol or acetone are used for the separation of proteins by
precipitation.
c) pH of the solution - influences the ionization state of proteins.
⇒ isoelecric pH (pHi or pI), at which the total electrical charge of the
protein is zero
⇒ solubility is minimal, the protein precipitation at pHi being a
method for protein precipitation and separation.
3. Properties related to the electric charge

• Ionisable groups (example –COOH, –NH2) ⇒ electric charge. Its magnitude

depends on:
• The number and the type of ionisable groups.
• Glu, Asp predominate ⇒ acidic character → acidic proteins.
• Lys, Hys, Arg predominate ⇒ the protein will be basic.
• at a pH < pHi, protein will be found in a cationic form (+);
• at a pH > pHi will be found in anionic form (-).

• The electrical charge of a protein is responsible of the conformation and

biological activity of the protein.
• Any modification of the physiological pH value will affect the electrical
charge of the protein, therefore its conformation and biological activity,
affecting the physiological process in which the protein is implied.

• Electrical charge used for protein separation:

• Electrophoresis
• Ion-change chromatography
4. Absorption of UV radiation
• Proteins solutions are colourless, except proteins that contain a coloured prosthetic
group (chromoproteins).
• Proteins absorb UV light, presenting a maximal absorption at 190 and 280 nm.
• The absorption pick at 190 nm is due to the peptide bonds, and the 280 nm pick is
due to the aromatic radical residues of thyrosine, phenylalanine, tryptophan

Absorption
Absorbţie Nucleic
Aciziacids
nucleici

Proteins
Proteine

220 240 260 280 300

Wave lenght
Lungime de undă
5. Hydrolysis

• braking of peptide bonds from the protein constitution with water.

• partial hydrolysis - part of peptide bonds are disrupted ⇒ smaller or larger
polypeptides;
• total hydrolysis - all peptides bonds are disrupted and proteins liberate
their amino acids.
• In organism, hydrolysis is used in the following processes:
• Hydrolysis of food proteins in the digestive tract.
• Hydrolysis of the proteins of the organism, during the catabolism or
regeneration process.

• Hydrolysis can be:

• enzymatic, under the catalytic action of the enzymes - peptidases.
• chemical - boiling the protein solution in a strong acidic or basic medium. The
process is scanty, certain amino acids being destroyed in this procedure, fact
that does not happen in the enzymatic hydrolysis.
6. Denaturation

• disorganizing of protein spatial structure, without affecting the primary

structure.
• disruption of bonds that contribute to the formation of protein
conformation.
• Denaturing agents:
• reducing agents can brake disulfide bonds S – S by (i.e. β-mercaptoethanol)
• Temperature - Most proteins suffer thermal denaturation, in a few minutes, at
temperatures between 50° and 80°C. Therefore, the increase of body
temperature with 5-6°C is fatale
• Chemical agents as: detergents, organic solvents that brake hydrophobic
bonds, or acids and bases that modify the protein electric charge.
• Heavy metal ions (Pb, Cd, Hg) bind the carboxyl and thiol groups.
• Urea, in 8M concentration, or guanidinium chlorhydrate in 6M concentration
are used as denaturating agents in the protein studies. These are hydrophilic
agents that disrupt the hydrogen bonds between water molecules and protein,
fact that produces protein precipitation.
• Physical agents as X, UV radiations, ultrasounds
• Denaturation modifies the following indicators of conformational integrity of
proteins:
• Entropy increases
• Ordered structure becomes disordered
• Solubility decreases, producing, usually, protein precipitation.
• Isoelectric pH value modifies, also the viscosity of protein solution
• Susceptibility to enzymatic hydrolysis increases. This aspect is used by the
organism during protein digestion at stomach level. Here, firstly proteins are
denatured by the action of hydrochloric acid 0.01M (pH=2), after that the
enzymatic hydrolysis takes place under the action of pepsin
Protein classification
Conformation

• Globular proteins contain different structural motives as α-helix, pleated sheet, bound between
by structures as β bend, or random structure that permits sudden modifications of direction,
characteristic to spheroid conformations.
• Examples of globular proteins: most albumins and globulins, globins in hemoglobin structure,
most plasma proteins, most enzymes and some membrane proteins.
• Most globular proteins are soluble in water and fulfil catalytic functions, transport or regulation
functions of metabolic pathways or gene expression.
• Fibrous proteins are formed of a single secondary structure (helix or pleated sheet), extended at
the level of the whole molecule. The conformation is of compact fibre, tightly wrapped up with
the other fibres.
• They are insoluble in water, with a good chemical and mechanical resistance ⇒ strength
structures of cells (cytoskeleton) or organism (bones, tendons, ligaments), or other protecting
structures: cell membrane, skin, nails, hair. Example: collagen, elastines, keratins.
Composition
• Simple proteins (holoproteins), constituted only of amino acids
• Conjugated proteins (heteroproteins), constituted of a holoprotein
bound to a non-proteic part or prosthetic group.
• Function of the prosthetic group nature, there are several types of
heteroproteins: metalloproteins, glycoproteins, lipoproteins,
phosphoproteins, chromoproteins and nucleoproteins.
Solubility
• Water and salt solution soluble:
• albumins - do not have a distinct amino acid (contain all type of amino
acids)
• globulins - no distinct amino acids.
• Water insoluble:
• prolamines - soluble in 70-80% ethanol, but insoluble in water and
absolute ethanol; arginine rich (form basic solutions)
• histones - soluble in salt solutions; low molecular weight (found in
DNA)
• scleroproteins - insoluble in water or salt solutions: rich in glycine,
alanine, proline (ex. collagens, elastines, keratins)
Holoproteins of Medical Importance
Vegetal proteins can be classified in four classes: prolamines, glutelins,
albumins and globulins. Prolamines are found only in vegetals. They are
poor in essential amino acids lysine and tryptophan, so they have an
incomplete dietary value. Albumins and globulins are rich in glutamic
and aspartic acids.
Animal globular holoproteins
Protamins are present in sperm cells
• small size (MW – 5000 – 10,000 dls).
• basic proteins and are soluble in ammonium hydroxide.
• form nucleoproteins with nucleic acids and are rich in Arg, Lys and His These
proteins lack Trp Tyr.
Histones are:
• very strong basic proteins as they are rich in Arg, Lys His.
• In combination with deoxyribonucleic acid (DNA) they form nucleoproteins or
more correctly nucleohistones which occur in cell nuclei forming chromatin
material.
• They are soluble in water but not in ammonium hydroxide.
• These proteins contain little or no Trp but Tyr is present.
• Small size - MW = 10,000 – 20,000 dls.
 Albumins and globulins

• Plasma proteins (6-8 g/100 mls) are a mixture of proteins,

which contain 10-15 main types and other 10-20000 minor
components.
• These proteins have important roles:
• maintenance of osmotic pressure (albumins);
• binding and transport of other molecules (lipoproteins, thyroxin
binding globulin, transferrin, etc);
• inhibitors of different proteases, liberated during diverse processes
(α1-antitripsin, α1-antichimotripsin α2-macroglobulin,
antithrombin, etc);
• antibodies (immunoglobulins or γ-gammaglobulins);
• coagulating factors.
• Plasma proteins are separated by electrophoresis, forming 5
migrating fractions:
• albumins (52-59%), and
• 4 types of globulins (α1- 3-5%, α2- 8-10%, β- 12-14% and γ- 16-
20%).
Albumins
• are water-soluble proteins.
• serum albumin (4.5 – 5.5 g/100 ml serum at humans), ovalbumin (eggs)
and lactalbumin (milk).
• coagulate when heated;
• Some of the albumins contain carbohydrate residues and are therefore not
simple proteins in the real sense.
• Hepatic cells synthesize serum albumin (12 g/day). If these cells are harmed
(i.e. in hepatitis), the concentration of serum albumin is less than normal.
• Structurally, it is a globular protein, formed of a single polypeptide chain
(585 amino acid residues) with the molecular weight 66,000.
• Albumin has t1/2 = 17 days.
• capacity to pass from blood to lymph.
• Contribute to osmotic pressure of plasma (80%). If albumin concentration
decreases dramatically, water accumulates into the interstitial space,
forming oedema.
• has binding sites for lots of compounds which circulate with the blood
attached to albumin (fatty acids, thyroxine, cortisol, hem, billirubin,
calcium, xenobiotics, including drugs.
Globulins
• are insoluble in water but soluble in dilute salt solutions
• Coagulate when heated.
• found in animals, e.g. lactoglobulin (milk), myosin in muscle, ovoglobulin
(eggs), serum globulins.
• more easily precipitated than albumins and this can be done by only half-
saturation with ammonium sulphate.
• The concentration of serum globulins is 1.5 – 3.5 g/100 ml serum.
• mixture of fractions that can be separated by electrophoresis (α1-, α2-, β-
and γ-globulins) and have importance in diagnosis.
• They achieve important roles:
• transporting globulins: α1-lipoprotein, ceruloplasmin, α2-retinol binding
protein, β-transferrin, β-transcobalamin;
• antiprotease globulins: α1-antitripsin, α2-macroglobulin;
• enzymes; α2-colinesterase, β-plasminogen;
• coagulating factors: α2-protrombine, β-factors V, VII, IX, X, XI, XII, XIII.
Immunoglobulins or antibodies

• five major classes: IgM, IgD, IgG, IgE and IgA

• two identical light (L) chains and two identical
heavy (H) chains
• Variable region. The H2N-terminal
• Hypervariable region
• Constant region
• Binding domain
•
The immunoglobulin can form polymeric structures, by polymerizing the base
structure: IgA – [(LH)2]2, IgM – [(LH)2]5.

Molecular Glucoside Serum conc.

Class Type (C/H)
weight % mg/100%

IgG 150,000 γ 53,000 2-3 600-1800

IgA# 170,000- α 64,000 7-12 90-420

720,000
IgD 160,000 δ 58,000 - 0.3-40

IgE 190,000 ε 75,000 10-12 0.01-0.10

IgM# 950,000 µ 70,000 10-12 50-190

Fibrous Holoproteins
• are high molecular weight proteins,
• characterized by a single type of secondary structure: α-helix (α-keratin,
myosin, troponin), β-pleated sheets (β-keratin), superhelix (collagen).
• According to their water-solubility, they can be divided into two categories:
• Fibrous, insoluble (schleroproteins)
• found in the conjunctive tissues, epithelial tissue
• roles as sustaining, protection, mechanical resistance.
• They are insoluble and resistant to hydrolysis.
• higher content in oxygen and a higher number of glycine, proline
and cysteine residues.
• The main schleroproteins are: collagens, elastins and keratins.
Except tropocollagen, which was already exposed, other examples
are reticulin in the lymph ganglions and vitrosin in the eye.
• Fibrous, soluble.
• contain a fibrous insoluble part, bounded to soluble, globular
domains. Ex. fibrinogen (blood coagulation), myosin (muscle)
Elastins
• fibrous protein that gives tissues and organs ability to stretch without
breaking, being elastic fibers in the ligament, vessel walls, etc.
• contain proline and hydroxyproline less than collagen but contain allysine
(derived from lysine)
• 3 residues of allysine and one lysine form cyclic structures - desmosine -
connecting the fibers of elastin.
• Elastins have no Gly-Pro repetitive sequences or Gly-X-Hyp and do not form
superhelix.
• Elastins have ordered secondary structure, containing disordered structures
in which amino acid residues are very mobile, which gives protein type
rubber elasticity.
Keratins
• Protein fibers in hair, skin and nails.
• Have a high chemical and mechanical resistance.
• Consist of one type of secondary structure: α-helix (α-keratin), β-sheet
folded (β-keratin).
• Their structure contains a segment of 7 amino acids repeated in tandem
type - (a - b - c - d - e - f - g) n -, where a and d are hydrophobic amino acids
and e and g are ionized polar amino acids.
• High content in cystein
• three-strand helix structure.
Fibrinogen is the fibrin precursor in blood clotting.
It is a big protein, MW = 340,000, formed of 3 pairs of polypeptide chains
(alpha, beta and gamma)
has α-helix structure and bound together by S-S bridges.
The three chains are also bound at one of the ends by globular domains.
Myosin is a component of thick filaments in striated muscles, cardiac,
skeletal, embryonic, and smooth muscle.
• It is formed of one pair of heavy chains (HC) and two pairs of light chains
(LC). In a given muscle fibre the 2 large subunits are identical, although
there are different HC isoforms in different types of muscle fibres.
• Heavy chains contain a long linear C-terminal α-helical domain and a
prominent globular N-terminal domain.
• also contains 4 relatively small proteins, which are associated with the
globular headpieces -alkali light chains (LC1 or LC3) and DTNB light chains
(LC2).
•.
 https://www.youtube.com/watch?v=GrHsiHazpsw
https://www.youtube.com/watch?v=BVcgO4p88AA
Tropomyosin is
• a long, rod-like, α,α-helically-interwound heterodimer,
• component of thin filaments in the striated muscle.
• It forms a superhelix structure.
• The two chains are bounded head to tail.

•
 Heteroproteins

• Complex proteins, formed of

• an apoprotein (a real protein structure, formed of linked amino acids)
• a prosthetic group, nonproteic, usually much smaller
• The prosthetic group confers catalytic properties (metallo-enzymes), is a
regulating factor (phosphorus-proteins), recognition and protection factor
(glycol- and lipo-proteins).
• The bonds established between the proteic part and the non-proteic one
depend on the nature of the non-proteic part.
• According to the prosthetic group structure, complex proteins are divided
into:
• chromoproteins - containing a coloured prosthetic group which can be a
porphyrin (ex. hemoglobin, cytochroms, catalase, peroxydase) or a riboflavine
(like visual protein rodopsine);
• glycoproteins
• lipoproteins
• phosphoproteins
• nucleoproteins
• metalloproteins
Phosphoproteins
• The vast majority of phosphorylations occur as a mechanism to regulate
the biological activity of a protein and as such are transient. In other words
a phosphate (or more than one in many cases) is added and later removed
– reversible process
• serine, threonine and tyrosine are the amino acids subject to
phosphorylation
• in glycogen synthase and glycogen phosphorylase in hepatocytes in
response to glucagon release from the pancreas, growth factors, signal
transduction proteins, etc
•
kinase

phosphatase
 Metalloproteins

• lots of proteins, especially enzymes, have one (or more) metal ion attached to the
protein.
• The metallic ion is chelated to the amino acid residues in the proteic part.
• Fe, Fe, Cu, Zn, Mg, Mn, Co, Se, etc.
• metal has a high contribution to the protein conformation but also can be
involved in protein function.
• Metalloproteins can have roles as:
• transport of metallic ions (transferrin for Fe2+ or ceruloplasmin for Cu2+)
• storing proteins (like ferritin for Fe2+)
• enzymes (ascorbate oxydase, monoamino oxydase – with Cu2+; carbonic anhydrase,
carboxypeptidase, alkaline phosphatase – with Zn2+;).
Glycoproteins
• covalently conjugated with carbohydrates.
• post-translational modifications.
• Glycoproteins are of two classes:
• N-linked sugars are attached to the amide nitrogen of the R-group of
asparagine;
• O-linked sugars are attached to the hydroxyl groups of either serine or
threonine and occasionally to the hydroxyl group of the modified
amino acid, hydroxylysine.

O-NAcGal bond N-NAcGlu bond

• N-linked families:
• 1. High-mannose type contains all mannose outside the core in varying
amounts.
• 2. Hybrid type contains various sugars and amino sugars.
• 3. Complex type is similar to the hybrid type, but in addition, contains
sialic acids to varying degrees. A variety of sialic acid is neuraminic acid
(NANA).

Ac HN H-OH COO H
H-OH
CH2 O H

H H H OH

OH H
• The number of carbohydrate groups attached to one or more points of polypeptide
chain is at least 12 to 15 residues.
• In some cases we have one single carbohydrate residue, eg submaxillary gland
glycoprotein (link α-N-acetyl-D-galactoseamine) or some types of collagen.

• In general, glycoproteins contain carbohydrate residues belonging to the series D,

except L-fucozei, L-arabinose and L-iduronic acid.
• The amount of carbohydrates can vary between 4% and 82% IgG in gastric
glycoprotein.

• Glycoproteins fulfill important functions in the body:

• cellular membrane glycoproteins is the external membrane receptor.
• It is the major component of mucus secreted by epithelial cells, mucus with
lubricating and protective role of the tissues of the gastrointestinal, respiratory and
urogenital tract.
• Some of the proteins are secreted glycoproteins, such as hormones like FSH, LH,
HCG and plasma proteins as orosomucoid, ceruloplasmin, plasminogen,
prothrombin, and immunoglobulins.
• modulate properties such as solubility, viscosity, electric charge, distortion.
• erythrocyte agglutination inhibitors containing blood group specific component.
• structural role (membrane glycoproteins).
A particular case is the glycoprotein haptoglobin.
• Proteoglycans
Compared to glycoproteins containing fewer carbohydrates
than protein, carbohydrate proteoglycans percentage exceeds
95% and therefore their properties are more like those of
polysaccharides.
• have as carbohydrates part - mucopolysaccharides.
• are predominantly components of extracellular matrices and
cell surface
• roles in cell adhesion and signaling in the cell.
Lipoproteins

• Structural complexes involving protein associated with lipids

(like phospholipids, cholesterol, triacylglycerol) via noncovalent
interactions (van der Waals, salt bonds) or covalent bonds are
termed lipoproteins. Proteins bind lipids by:
• Protein acylation at the level of amino residues of protein with
miristoyl, palmitoyl residues
• Non polar bonds van der Waals
• Ionic bonds between O-PO32- and +HN(CH3)3 in phosphatides and –NH3+
or, respectively, with –COO- in proteins.
After localization, lipoproteins can be divided:
• Structural Lipoproteins in cell membranes and cell organelles, the
role of isolation and permeability.
• Plasma Lipoproteins, involved in lipid transport, hydrophobic
hormones, vitamins and drugs in serum. Depending on the density
they are divided into: chylomicrons, VLDL, IDL, LDL and HDL.
Nucleoproteins
• Nucleoproteins are heteroproteins formed of apoproteins (protamins and histones)
and the prosthetic group – nucleic acids (DNA and RNA).
• Nucleic acids are polymers of nucleotides.
• They are responsible for the storage and passage of information needed for the
production of proteins.
• Nucleic acids are found in two basic structural forms:
• deoxyribonucleic acid (DNA) - serves as the genetic material.
• ribonucleic acid (RNA) which plays multiple roles:
• genetic material for some viruses (e.g. tobacco mosaic virus, poliovirus, influenza virus).
• carrier of genetic information to the site of protein synthesis (messenger RNA)
• forms the crucial link between messenger RNA and amino acids, being coupled in protein
synthesis (transfer RNA).
• RNA is an essential component of ribosomes and some enzymes. In fact RNA can have
catalytic activity without interacting with proteins.
• Nucleoproteins have role in:
• cell division
• proteins biosynthesis
• transmission of hereditary characters
 Nucleoprotein

Holoproteins Nucleic acid

(protamines, histones, (polynucleotide)
basic character, low
molecular weight)
Mononucleotide

Nucleoside Phosphoric acid

Nitrogenous Pentose
base

Purine Pyrimidine Ribose Deoxyribose

• Pentoses in nucleic acid constitution are ribose (RNA) and
deoxyribose (DNA), both being the β-anomer.

5
H O C H2 O OH H OCH 2 O OH

4 1
H H H H
H H H H
3 2

OH OH OH H
ribose deoxyribose
Nitrogenous bases

Purine Pyrimidine

purine bases: adenine and guanine, abbreviations A, G

pyrimidine bases: thymine, cytosine and uracil, abbreviations T, C, U

• The purine and pyrimidine bases have two structural tautomere forms;
• lactim – the hydroxy form (or amino), and
• lactam – the oxy (or imino) form.
• In cells, they appear practically only in the lactam and amino structures.

OH O
NH2 NH

N HN
N N HN N

HO N O N
N N N N
H H H

lactim lactam amino imino

• Pyrimidines:

OH O
NH2 NH2

N HN
N N

HO N O N
H HO N O N
Lactim Lactam H
Uracil Lactim Lactam
(2,4 - dihidroxi - pirimidina) Citozina
(2-hidroxi-4-amino-pirimidina)

OH O

CH3 CH3
N HN

HO N O N
H
Lactim Lactam
Timina
(5 - metil-uracil)
• Purines:
NH2 NH
6 7
5 N N N
1N N HN
8
2
N 4 N N N N N
3 H H H
9
Adenina (imino)
Purina
(6 - aminopurina)
(amino)
lactim lactam
OH O NH2

N N N
N HN N

H2N N N H2N N N HO N N
H H H
Guanina Izoguanina
(2 amino - 6 - hidroxi -purina) (2 - hidroxi - 6 - amino -purina)

• During purines
O metabolism: O O
H
N N N
HN HN HN
O

N N H2O O N N H2O O N N
H 2H H H 2H H H
Hipoxantină Xantină Acid uric
Nucleosides
• Resulte by condensation of a nitrogenous base (purine orpyrimidine) with a
pentose (ribose or deoxyribose, furanosic form, anomere β).
• - N-glycosidic bond (C1 or C9)

O NH2 NH2 OH
N N
HN
H N N N N
1 1 9 9
O N O N N N H2N N N

5' 5' 5'

HO CH2 O HO O HO CH2 O O
CH2 HO CH2
4' 1' 4' 1' 4' 1'
H H H H H H H H
H 3' 2' H 3' 2' H 3' 2'
H H H H H
OH OH OH H OH OH OH H
Ribouridina Dezoxiribocitidina Riboadenozina Dezoxiriboguanozina
• Nucleotides
• Esters of nucleosides with phosphoric acid at C3` or C5`, usually at C5`
• Can exist as free compounds or DNA or RNA residues
• Have acidic properties due to phosphate residue
• ⇒ adenosine monophosphoric acid or adenylic acid (AMP), etc

NH2
N
N

N N

O CH2 O
HO P

OH H H
H H

OH OH
AMP
Adenozin 5' - monofosfat
• The base can exist in 2 distinct orientations about the N-glycosidic bond.
These conformations are identified as, syn and anti. It is the anti
conformation that predominates in naturally occurring nucleotides

syn-Adenosine anti-Adenosine
 Nucleoside and Nucleotide Structure and Nomenclature

Nucleoside
Nucleotide
Base Formula Base (X=H) X=ribose or
X=ribose phosphate
deoxyribose

Cytidine monophosphate
Cytosine, C Cytidine, A
CMP

Uridine monophosphate
Uracil, U Uridine, U
UMP

Thymidine
Thymine, T Thymidine, T monophosphate
TMP

Adenosine
Adenine, A Adenosine, A monophosphate
AMP

Guanosine
Guanine, G Guanosine, G monophosphate
GMP
• The nucleotides found in DNA are unique from those of RNA in
that the ribose exists in the 2'-deoxy form and the
abbreviations of the nucleotides contain a d designation. The
monophosphorylated form of adenosine found in DNA
(deoxyadenosine-5'-monophosphate) is written as dAMP.
• The nucleotide uridine is never found in DNA and thymine is
almost exclusively found in DNA.
• Thymine is found in tRNAs but not rRNAs nor mRNAs. There
are several less common bases found in DNA and RNA.
• The primary modified base in DNA is 5-methylcytosine. A
variety of modified bases appear in the tRNAs.
• Many modified nucleotides are encountered outside of the
context of DNA and RNA that serve important biological
functions.
• Nucleotides can exist in the mono-, di-, or tri-phosphorylated
forms.
• Nucleotides are given distinct abbreviations
• The monophosphorylated form of adenosine (adenosine-5'-
monophosphate) is written as, AMP.
• The di- and tri-phosphorylated forms are written as, ADP and
ATP, respectively.
• The use of these abbreviations assumes that the nucleotide is
in the 5'-phosphorylated form.
• The di- and tri-phosphates of nucleotides are linked by acid
anhydride bonds.
• Acid anhydride bonds have a high ΔG0' for hydrolysis imparting
upon them a high potential to transfer the phosphates to other
molecules (macroergic).
• It is this property of the nucleotides that results in their
involvement in group transfer reactions in the cell.
Chromoproteins

• They are heteroproteins with a coloured prosthetic group.

• Function of the nature of the prosthetic group, the chromoproteins can be
classified as:
• Porphyrinic chromoproteins – their prosthetic group is the heme, in
different variants (heme is a derivative of the porphyrinic nucleus). The
main proteins in this group are:
• Hemoglobin
• Myoglobin
• Cytochroms
• Chlorophylls
• Porphyrinic enzymes: catalase, peroxidase.
• Non porphyrinic chromoproteins – the prosthetic group is different of
heme. The main proteins in this group are:
• Caroteno-proteins – for example visual pigments;
• Flavoproteins – for example enzymes with enzymatic cofactor
derivatives of vitamin B2 (FMN and FAD).