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Protein Architecture
Protein Architecture
Topic:
General characteristics of
Proteins as polymers of L-amino acids
Diverse molecular weight
Diverse functions
Unique three-dimensial shape
Distribution of proteins in tissues
A receptor
globular proteins
which are water and salt
solution soluble.
Topic:
Globular proteins
as the enormous class of proteins, abundant,
bioactive and essential for most of metabolic
processes.
Globular proteins
Serum albumin
Myoglobin, hemoglobin,
Immunoglobulins,
Some peptide hormones,
Cellular receptors,
Cytokines,
Transferrin,
Ceruloplasmin,
Glycoproteins, lipoproteins,
phosphoproteins.
Globular
proteins
Globular proteins
are so named,
because
their
polypeptide
chains
are folded into
compact
structures,
very unlike the
extended,
filamentous
forms of the
fibrous
proteins
Fibrilar proteins
Interior:
Core
of a protein
Surface
of a protein
Arg, His, Lys,
Asp, and Glu
H2O
Surfaces of globular
proteins are coated
by water molecules
Red:
Hydrophobic aa
Green:
Hydrophilic aa
Membrane
proteins
are classified
according to
how tighly
they are
associated
with
membranes
GPI
Peripheral protein
Integral
proteins
cy t o p l a sm
Peripheral protein
Peripheral
protein
is loosely
anchored in
membrane by
hydrophobic,
helical
C-terminal
segment.
GPI-anchor
Some protein are anchored to the membrane
by covalent type linkage named
Glycosyl-Phosphatidyl-Inositol, (GPI) anchor.
GPI- anchor
Protein
Ma
n
Man
Man
GlcN
Cell surface
CYTOPLASM
Enzymatic hydrolysis)
GPI-PLD
Man
Man
Man
GlcN
Cell surface
GPI-PLC
cytoplasm
13
Enzymatic hydrolysis)
GPI-PLD
Man
Man
Man
GlcN
Cell surface
GPI-PLC
cytoplasm
13
GPI-anchored protein:
Primary
level
Secondary
Tertiary
Quaternary
Rigid and
planar
peptide
bonds
between aa
create a
backbone of
a polypeptide
chain
vasopressin
oxytocin
Both hormones are used as a drugs, vasopressin to
combat loss of blood pressure after surgery, while
oxytocin to induce labor.
The electrophoretic
pattern of Hb from
normal individuals and
those with sickle cell
anemia:
Normal erythrocytes:
Secondary structure
Lineus
Pauling
1954
Nobel
Price
The helix
Unregular secondary
structure
Non-repetitive
structures
random coil or
loop conformation
i.e. regions
(segments)
disordered,
and bulges
supersecondary structures
They occur in many globular proteins.
Leucine zipper
Spatial structural protein motif which
contains leucines
Wikipedia modified
Superstructures (motifs)
in proteins
build from -pleated sheets:
Beta meander
Twisted sheets
Ribbon sheets
Beta sandwich
Cylinders
Beta barrels
consists of an antiparallel
sheet formed by sequential
segments of polypeptide
chain, that are connected
by relatively tight reserve
turns
Two units
of parallel and antiparallel structures
are joined together by segment of
hairpin:
The pleated
antiparallel sheets
loop is compact
globular entities, they
side chains tend to fill
in their internal
cavities.
loops are almost
invariably located on
the protein surface,
they may have
an important role in
biological recognition
process
More stick figure that turns
It is folding of
polypeptide, that gives
the molecule its overall
three dimensional
shape.
Proteins
are folded into
compact structures
Tertiary
Hydrogen bonding
Ionic
interactions
Hydrophobic
interactions
Disulphide bridges
Intra-S-S
Inter-SS-
A secondary
A tertiary
A quaternary
Topic
Mosaic proteins and multidomain proteins
A mosaic proteins:
6
1
2
Type I, II, III segments
EDA
EDB
RGD
PHSRN
IIICS
COOH
NH2
Some sequences/modules
of large polypeptides can form
domains:
Polypeptide chains that consist of more than ~200
aa usually fold into two or more globular clusters
known as
domains,
Domains of
proteins
Domain: A large
polypeptide chain
is often locally folded
into globular clusters
The domains
give the protein
multiglobal
appearance
FN I
sushi
FN II
FN III
Coagulation
factor V
Immunoglobulin-like
Many
domains
are
present
in
multiple
copies in
their
parent
proteins
Lipoproteins
Lipids
Glycoproteins
Sugar/s, glycan/s
Nucleoproteins
Nucleic acid
Heme proteins
Heme
Metalloproteins
Phosphoproteins
Phosphatic acid.
Topic
THE GLYCOPROTEINS
Glycation
Seminar
can mainly undergo hemoglobin,
albumin, some membrane proteins, and nervous
system proteins, some matrix proteins (collagen),
Protein
Protein
Glucose
Protein
Protein
Protein
Glycoproteins
Subclasses of glycoproteins:
N-, O- glycoproteins
Mucins
Proteoglycans
Peptydoglycans in bacteria
N- and O- glycoproteins:
Two ways
of bonding
oligosaccharide
chains (glycans) with
proteins to form
glycoprotein:
Asn
Protein
chain
N-glycoproteins:
N-AcGlc and an asparagine
Thr or
Ser
N-glycosidic bond
O-glycosidic bond
Protein
chain
O-glycoproteins:
N-AcGlc/N-AcGal and
serine or threonine
Microheterogenetic forms
of N-glycans attached to
the same protein part
are called glycoforms
In living organism
You can find
TetraDiTridifferent glycoforms
building
this same
glycoprotein.
The distribution of
glycoprotein
glycoforms is stable
Glycoforms1,2,3
in physiological state
Glycoproteins
microheterogeneity
depending on type of
glycans
attached to their
protein part
IMPORTANT:
The distribution
of glycoprotein glycoforms
is stable
in physiological state of human organism
Signalling
Degradation
Apoptosis
Topic
Other distinct family
of O-linked glycoproteins
are
THE MUCINS
Cysteine region
MUC2
MUC1
Topic
PROTEOGLYCANS
are essential parts of
tissues of
skin, cartilage,
cornea of the eye
where they provide
strength, flexebility,
and elasticity
The proteoglycans
are special class of glycoproteins:
They have
a protein core,
and
a long polysaccharide chains (80%)
made of acidic glucosaminoglycans
(GAG)
Structure of proteoglycans
Glucosoaminoglycans (GAG) chains are
usually bound to the protein core
through either short oligosaccharide linkage
Xyl, Gal, GalNAc, GlcNAc,
Protein part-Ser-O- b1-Xyl-Gal-GalNAc-GlcNAcLinkage
b1-4 repeating units of chondroitin,
dermatan, heparan-sulfates
Topic
LIPOPROTEINS
Lipoproteins particles
consits of noncovalently associated
lipids and proteins.
Lipoproteins function in the blood plasma:
transport vehicles for triacylglycerols and
cholesterol.
Plasma lipoproteins
form globular micelle like particles,
that consists of:
triacylglycerols,
cholesteryl esters,
proteins,
phospholipids,
cholesterols.
Plasma lipoproteins
cholesterol
protein,
cholesterol
Triacylglycerols,
cholesteryl esters
phospholipid
protein
protein
cholesterol
phospholipid
nonpolar core
surrounded by
an amphiphilic
coating of
Lipoproteins
have been classified into five broad
categories on the basis
of their functional and physical properties:
1. Chylomicrons
2. Very low density lipoproteins:
VLDL
3. Intermediate density
lipoproteins: IDL
4. Low density lipoproteins: LDL
5. High density lipoproteins: HDL
Protei
n
Basic function of
Very low density lipoproteins VLDL,
Intermediate density lipoproteins
IDL,
Low density lipoproteins LDL is:
Transport of endogenous
(internally supplied: the liver synthesizes
triacylglycerols from excess
carbohydrates)
triacylglycerols
and cholesterol
from the liver to the tissue
The HDL: