BIOCHEMISTRY 08/22/2019

Amino Acids, Peptides and Proteins Shifting #1

Trans #2
Dr. Phyllis Rio
[SUBJECT]
[Name of Lecturer]
OUTLINE

I. Amino Acids C. Structures

A. Classification D. Protein Folding
B. Properties E. Complex Proteins
[Name of Lecturer]
C. Chemical
Reactions III. Clinical Significance
[SUBJECT]
D. Special Function
II. Proteins
Figure 2. Proline structure
[Name
A. How of Lecturer]
to draw a
peptide bond
B. Characteristics of A. CLASSIFICATION
a[SUBJECT]
peptide bond
BASED ON STRUCTURE
I. AMINO ACIDS
• Aliphatic (w/o benzene)
• The building blocks of proteins à Monoamino monocarboxyl
à Monomer units from which the long 1. Simple – Alanine & Glycine
polypeptide chains of proteins are synthesized 2. Branched – Isoleucine, Leucine, & Valine
• 300 amino acids are naturally occurring, but only 20 3. Hydroxylic – Serine & Threonine
commonly occurring amino acids are recognized in protein 4. Sulfur-Containing – Cysteine & Methionine
which codes for by the DNA 5. Carboxamide – Asparagine & Glutamine
à Monoamino dicarboxyl (Acidic – Negative charged)
SELENOCYSTEINE o Aspartic acid & Glutamic acid
• The 21st amino acid à Diamino monocarboxyl (Basic – Positive charged)
• L-a-amino acid in peroxidases and reductases o Arginine & Lysine
à for the catalysis of electron transport • Aromatic (w/ benzene) & Heterocyclic (w/ ring)
reactions à Histidine (Diamino monocarboxyl), Phenylalanine,
• Selenium atom replaces sulfur of its structural analog, Proline, Tryptophan, & Tyrosine (Hydroxylic)
cysteine
• Inserted in polypeptide during translation BASED ON SIDE CHAIN
• No codons are specified for it • Non-polar (Hydrophobic except Glycine)
à Located at the interior part of protein domains
BASIC STRUCTURE à Electrons equally shared between atoms in side chain
à Mnemonic: Go And Take Vital Part In Promoting Mother
• Main components
Language
à Central carbon
à Glycine, Alanine, Tryptophan, Valine, Proline,
à Amino group (-NH2)
Isoleucine, Phenylalanine, Methionine, & Leucine
à Carboxyl group (COOH-)
à Hydrogen atom • Polar (Hydrophilic except Tyrosine)
à Variable R group (side chain) à Located at the exterior part of protein domains
à Uncharged side chain
o Mnemonic: Some Times Cats Try A Growl
o Serine, Threonine, Cysteine, Tyrosine,
Asparagine, & Glutamine
à Charged side chain
o Mnemonic: A Good Lawyer Aims High
o Aspartic acid, Glutamic acid, Lysine, Arginine,
Histidine
• Special Groups (see Appendix for diagram)
à Arginine – Guanidinium group
à Histidine – Imidazole ring
à Phenylalanine – Benzene ring
à Proline – Pyrrolidine ring
Figure 1. General structure of an amino acid à Tryptophan – Indole ring
à Tyrosine – Phenol
Proline
• Amino group is not separated from the R group as it is part BASED ON METABOLIC FATE
of the pyrrolidine ring • Glucogenic
• Imino acid – derivatized imine group + carboxylic acid à Amino acids that can be converted into glucose,
pyruvate, or some glycolytic intermediates (e.g. α-
Ketoglutarate, Oxaloacetate)
à May enter the glycolytic pathway if converted to
glucose
• Ketogenic
à Amino acids that can be converted to ketone bodies that
will be later converted to acetyl-CoA
à Does not enter the glycolytic pathway
à The two “Ls” – Leucine and Lysine
BCHM Abara, Baldeo, Cruz, Donato, Gomez, Mariano, Padaon, Potenciano, Suarez, Tabungar. 1 of 8
• Both Glucogenic and Ketogenic o Both carboxyl group are unprotonated
à Could generate the products of both pathway o Net charge of -1

Figure 5. Amino Acid at physiological pH, Zwitterion state

• Ionization state of AA varies with pH

® In acidic solution, the amino group is protonated ( - NH3+ )
and carboxyl group is not dissociated (COOH); cationic form
® In basic solution they are anionic form

Figure 3. Metabolic fates of amino acids.

Figure 6. Ionization based on pH
BASED ON NUTRITIONAL REQUIREMENT
• Essential ISOELECTRIC POINT
à Cannot be synthesized by the body • pKa
à Must be obtained through nutritional intake ® Dissociation constant
à Mnemonic: PVT TIM HALL ® Acidic strength of the carboxyl, amino and ionizable R
à Phenylalanine, Valine, Threonine, Tryptophan, groups in AA
Isoleucine, Methionine, Histidine, Arginine (Only essential § pk1 – carboxyl group
for developing infants), Leucine, & Lysine § pk2 – amino group
• Non-Essential • Net charge of AA depends upon the pH of medium;
à Can be sythesized by the body ® As pH changes so do the charges
à The other 10 remaining amino acids or you can use the ® Observed during titration
Mnemonic: Almost All Girls Go Crazy After Getting Taken ® Isoelectric point (pI)- net charge is zero
Prom Shopping
à Alanine, Asparagine, Glutamic acid, Glutamine,
Cysteine, Aspartic acid, Glycine, Tyrosine, Proline, &
Serine
B. PROPERTIES

• All have high melting points

• All are soluble in polar solvent (water and alcohol) but
insoluble in nonpolar solvent (benzene)

ACID-BASE PROPERTY
• AA have both the acidic, carboxyl group (α -COOH) and basic,
amino group (α-NH2) components
• These groups are capable of ionizing
• As R-groups of acidic and basic AA as well as Cysteine and
Tyrosine
• Carboxylic group is more acidic than amino group; it gives off
H+ first Figure 7. Ionization state at different pH

Figure 4. Hydrogen dissociation of carboxyl group (top) and amino group

(bottom)
• At physiological pH (7.4)
® Carboxyl group is unprotonated (COO-) and amino group
(NH3+) is protonated
® Zwitterion
o AA has no ionizable R group, it is electrically neutral at
7.4 pH and in dipolar form Figure 8. Titration of alanine with hydroxide
o Ampholytes or amphoteric substance
® Monoamino dicarboxylic AA • pH at which the net electrical charge of the AA is 0; no charge
o Amino group is pronated

BCHM Amino Acids, Peptides and Proteins 2 of 8

• All the groups are ionized but cancel each other; no mobility of
field
• Solubility and buffering capacity will be MINIMUM; less
interaction in water due to absence of positive and negative
charge
• pI =𝒑𝑲𝒂𝟏+𝒑𝑲𝒂𝟐/𝟐
® pk1 – carboxyl group
® pk2 – amino group
• AA pKa values range: -1→ 0 → +1
Figure 11. Decarboxylation of Tyrosine
OPTICAL PROPERTY
• AA are chiral; the tetrahedral carbon with 4 different substituents 2. AMIDE FORMATION
• Glycine in NOT chiral since its R-group is hydrogen atom • Dicarboxylic amino acids (Asp and Glu)
• Chirality • Carboxyl group (not α-carbon carboxyl group)
combines with ammonia
® Describes the handedness of the molecule
• e.g. Aspartic acid + NH3 Asparagine
® Refers to the ability to rotate the plane of polarized light
Glutamic acid + NH3 Glutamine
§ Dextrotatory, D configuration- to the right
§ levorotatory, L configuration- to the left
® All AA are L configuration except Glycine
® D amino acids are never found in proteins, exist in nature,
often found in antibiotics

Figure 12. Glutamic acid undergoes amide formation forming Glutamine

Figure 9. Amino Acid Configuration
REACTIONS INVOLVING THE AMINO GROUP
LIGHT ABSORBENT PROPERTY
1. TRANSAMINATION
• AA do not absorb visible light • Transfer of the α-amino group to an α-keto acid
• Aromatic AA - Tryptophan, Tyrosine, Phenylalanine can to form a new amino acid and a new α-keto acid
absorb UV light • e.g. α-ketoglutarate + alanine glutamic
• Tryptophan acid + pyruvate
® absorbs UV light more efficiently than Tyrosine/Phenylalanine,
and its predominance in most proteins causes them to have
the ability of absorb UV light.

Figure 13. Transamination of Alanine

2. OXIDATIVE DEAMINATION
• α-amino group is removed from an amino acid to
form a ketoacid and ammonia
• Glutamic acid is the most common amino acid
that undergoes this reaction

Figure 10. Ultraviolet absorption spectra of tryptophan, tyrosine, and

phenylalanine.

C. CHEMICAL REACTIONS

REACTIONS INVOLVING THE CARBOXYL GROUP

1. DECARBOXYLATION
Figure 14. Oxidative deaminatiion of Glutamic acid to form α-ketoglutarate
• Removal of the carboxyl group
• Produces important amines and carbon dioxide 3. FORMATION OF CARBAMINO COMPOUND
• e.g. HISTIDINE Histamine and Carbon • Mechanism by which CO2 is removed from
dioxide tissues to lungs via blood
TYROSINE Tyramine and Carbon • Carbon dioxide will react with α-amino group at
dioxide alkaline pH

BCHM Amino Acids, Peptides and Proteins 3 of 8

 Figure 15. General reaction for carbamino compound formation
REACTIONS INVOLVING THE SIDE CHAIN
1. TRANSMETHYLATION
• Involes methyl group of methionine Figure 19. Formation of Cystine
• Removal of the methyl group and transfers it to D. SPECIAL FUNCTIONS
cysteine which will result in the formation of
homocysteine Table 1. Derivatives of amino acids and their functions
Amino acid
Derivative Function
precursor
Ornithine and Essential for urea
Arginine
citrulline synthesis
Carrier of ammonia
and of the carbons
Alanine - of pyruvate from
skeletal muscle to
liver
Conditional
Cysteine Taurine essential amino
acid
Glutamic acid and
Gamma amino
dopamine (from Neurotransmitter
butyric acid (GABA)
Figure 16. Transmethylation of Methionine forming Homocysteine tyrosine)
Mediator of allergic
2. ESTER FORMATION BY -OH GROUP Histamine reaction and acid
• Involves hydroxy amino acids secretion
• Hydroxyl groups of serine, threonine and Histidine
Buffering activity
tyrosine, form esters with phosphoric acid to - (Can donate or
produce phosphoproteins accept protons)
Binding of
coenzymes like
Lysine -
pyridoxal phosphate
and biotin
Production of S-
adenosylmethionine
Methionine -
(Biosynthesis of
polyamines)
Biosynthesis of
Serine -
sphingosine
Thyroxine and
Figure 17. General reaction of phosphoprotein formation. Thyroid hormones
Triiodothyronine
3. REACTION OF AN AMINO GROUP Alpha and Beta
• Amide groups of glutamine and asparagine can Tyrosine Epinephrine and adrenergic
form N-glycosidic bonds with carbohydrates to Norepinephrine (Vasoconstrictor,
form glycoproteins Bronchodilator)
Dopamine Neurotransmitter
Tryptophan Serotonin Neurotransmitter

Figure 18. Formation of N-glycosidic bond between Asparagine and N-
acetylglucosamine forming a glycoprotein
4. REACTION OF SULFHYDRYL GROUP
• Sulfhydryl group of cysteine forms a disulfide
(S-S) bond with another cysteine to form cystine
II. PROTEINS
• Macromolecules with nitrogenous compounds
• Peptide – short chain of amino acid
• Peptides are used as:
1. Hormones (e.g. insulin)
2. Neurotransmitters (e.g. GABA)
3. Antibiotics (e.g. Gramicidin A)
4. Regulators (e.g. Glutathione)
5. Anti-tumor agent (e.g. Belomycin)
• By convention, N-terminal end is written at the left while
the C-terminal end is written at the right.
• Polymerization of amino acids through peptide bonds to
form the structural framework of proteins
• Protein – long chain of amino acids

BCHM Amino Acids, Peptides and Proteins 4 of 8

Peptide bond formation
• Most important reaction of amino acids
• Also called “Amide bond”
• Formed when a-carboxyl group of one amino acid reacts
and condenses (non-enzymatically) with a-amino group of
another amino acid with loss of water
• A covalent bond resulting to stable sharing of electrons
• CO-NH bridge
Figure 20. Peptide bond
• # of peptide bonds - # of AA residues minus one
à a 3 amino acid residue (a tripeptide) will form
2 peptide bonds
• In mammals, peptide hormones typically contain only the
a-amino acids of protein linked by a peptide bond
• Other peptides contain non-protein amino acids,
derivatives of amino acids, or amino acids linked by an
atypical peptide bond.
à The amino terminal glutamate of glutathione,
a tripeptide that participates in the metabolism of
xenobiotics and the reduction of disulfide bonds,
is linked to cysteine by a non-a peptide bond.
Figure 21. Glutathione structure
A. HOW TO DRAW A PEPTIDE BOND
1. Use a zig-zag to represent the main chain or backbone
(HN-CH-C=O). By convention, peptides are written with
the residue that bears the free a-amino group at the left.
2. Add the main chain atoms: a-nitrogen, a-carbon, carbonyl
carbon
3. Add a hydrogen atom to each a-carbon and to each
peptide nitrogen, and an oxygen to the carbonyl carbon
4. Add the appropriate R groups to each a-carbon atom
5. Three-letter abbreviations linked by straight lines
represent an unambiguous primary structure. Lines are
omitted for single letter abbreviations.
• Example: Asp-Ala-Ser
B. CHARACTERISTICS OF A PEPTIDE BOND
• It is partial double bond, no freedom of rotation
• It is rigid and planar (O, C, N, and H atoms of a peptide
bond are coplanar)
• It is trans in nature (except Proline)
à R-groups are on opposite sides of an
imaginary reference line on the molecule
à Less steric effect from bulk R- groups and
less energy needed to maintain structure which
makes it more stable
• Side chains are free to rotate on either side of peptide
bond
• Peptide Bond has partial double-bond character
BCHM Amino Acids, Peptides and Proteins
à There is no freedom of rotation about the
bond that connects the carboxyl carbon and the
nitrogen of a peptide bond
à The imposed semi-rigidity of peptide bonds
has important consequences for higher orders of
protein structures
• Non-covalent forces constrain peptide conformations
à Hydrogen bond and hydrophobic interactions
• Peptides are Polyelectrolytes
à Peptide bond is uncharged at any pH of
physiologic interest
à Formation of peptide is accompanied by a net loss
of 1 positive and 1 negative charge per peptide bond
formed
à Peptides are charged molecules at physiologic pH
owing to their -COOH and -NH3 terminal groups, and,
where present, their acidic or basic R groups
• For amino acids, the net charge on a peptide depends on
the pH of its environment and pKa values of dissociating
groups
C. STRUCTURES
Configuration
• geometric relationship between a given set of atoms
• L- and D-amino acids or L- and D-isomers
Conformation
• spatial relationship of every atom in a molecule
• three-dimensional arrangement
• interconversion between conformers occurs without
covalent bond rupture
Rotation about a single bond
• Proteins have different levels of structural organization:
à primary, secondary, tertiary and quaternary
• Folding:
à amino acids are of the opposite charge to attract each
other and form ionic bonds
PRIMARY STRUCTURE
• Denotes the number and sequence of amino acids in
protein
• Polymerization of amino acids – polypeptide chain
• Each amino acid in the chain is called a residue
• Structure is linear and linkage is maintained by peptide
bond
• Higher levels of organization are decided by primary
structure
à Primary structure determines biologic activity
à Polypeptide chain has unique amino acid sequence
decided by gene sequence as encoded in the genetic
code
à Gene codes not only determine the order of amino
acids in a protein, but they also determine a protein's
structure and function
à When sequence is changed, polypeptide is also
changed
à A single amino acid change (mutation) in a linear
sequence may have profound effect on the function
à Example in normal hemoglobin (Hb A); amino acid in
the beta chain – glutamic acid but in sickle cell anemia it
is changed to valine
Regular Conformations in Protein
• Two broad classes:
1. Globular
• Compactly folded and coiled
• For catalytic, regulatory, and transport functions
2. Fibrous
• More filamentous or elongated
• For structural and contraction functions
5 of 8
SECONDARY STRUCTURE
• Protein or portions of protein exhibit regularly repeating
types of structures
• Two common regular conformations – alpha helix and
beta pleated sheet
• Stabilized by hydrogen bond
à formed between the carbonyl group one amino acid to
amide group of another amino acid
à occurs between one of the lone pairs on an oxygen
atom of carbonyl group and the hydrogen attached to a
nitrogen group

Figure 23. a-helix structure

Figure 22. Secondary Structure of Protein
TYPES OF SECONDARY STRUCTURE
1. a-helix
• common structure of globular class
• Coiled / spiral with rod-like structure
• Tightly coiled backbone forms the inner part of
the rod and side chains extend outward
• Stabilized by intrachain hydrogen bonds
• Carbonyl carbon (CO) of one amino acid forms
H bond with amine nitrogen (NH) of another
amino acid that is situated four residues ahead
in the sequence
• Right-handed alpha helix: more stable
• Favor alpha helix: alanine, aspartic acid,
glutamic acid, leucine, isoleucine, methionine
• Disrupts helix (produces bend): glycine and
proline
• Structures with alpha helix: keratin, collagen,
fibrin
PARTS OF AN a-HELIX STRUCTURE:
• Pitch – the vertical distance in one turn
o There are 3.6 residues per turn (13 atoms)
• Rise – distance between amino acids
2. β- Pleated Sheets
• Composed of two or more of different regions
stretches of at least 5 – 10 amino acids (beta
strands)
• Beta strands are extended polypeptide chains
• Chains are folded so that they lie alongside
each other
• Beta sheet is formed by linking two or more beta
strands by interchain hydrogen bond
• These are pleated due to positioning of the alpha
carbons of peptide bond which alternates above
and below the plane of sheet
• Types of β-pleated Sheet
à Parallel: adjacent peptide chains proceed in
the same direction
à Antiparallel: adjacent chains are aligned in
opposite direction
Figure 24. Different b-pleated sheets
SUPERSECONDARY STRUCTURES
• Intermediate in scale between secondary and tertiary
structures.
• Include loops, turns, bends, and other extended
conformational features.
• E.g. structural motifs (repetitive or non-repetitive) such as
the helix-loop-helix motif or the E-F hands of calmodulin.
• Turns and bends
à Short segments of amino acids that join units
of the secondary structure, such as two adjacent
strands of an antiparallel β sheet.
à β turns involves four aminoacyl residues
à Proline and glycine often present in β turns

BCHM Amino Acids, Peptides and Proteins 6 of 8

 • Loops unequal distribution of electron or an
à Short regions that contain residues beyond electric dipole.
the minimum necessary to connect adjacent 4. Disulfide Bond
regions of 2nd structure • Covalent bonding between the "R"
• Loops and bends reside on surface of protein and serve groups of cysteine amino acids.
as readily accesible site ( epitopes ) for binding of • Many extracellular proteins contain
antibodies disulfide bonds
TERTIARY STRUCTURE
• Refers to the entire three-dimensional conformation of a
polypeptide.
• Describes the spatial relationship of different secondary
structural features - helices, sheets, bend, turns, and loops
- assemble to form domains.
• Domain – section of a protein structure sufficient to
perform a particular chemical or physical task such as
binding of a substrate or other ligand.
• Chaperone - assist the covalent folding or unfolding and
the assembly or disassembly of protein
• Incorrect folding may produce an alteration in protein
structure (Prion Disease).
• Important features of the tertiary structure: Figure 25. Bonds forming the tertiary structure
1. Interior-amino acids with hydrophobic side
chains/ R groups QUATERNARY STRUCTURE
2. Exterior/surface- hydrophilic amino acids • Multiple polypeptide chains assembled into oligomeric
interacting with aqueous environment proteins.
• Stabilized by same forces that hold tertiary structures
Bonds Forming the Tertiary Structure
• Describes the arrangement and position of each of the
• Interaction between R groups of the amino acids would subunits in a multiunit protein.
favor formation of additional hydrophobic bond, hydrogen • Major stabilizing force of quaternary structure -
bond, ionic/ electrostatic bonds, Van der Waals forces and Hydrophobic interaction.
disulfide bridge • Types of Quaternary Structures:
• Non-covalent bond a. Homo-oligomers – with identical subunits
1. Hydrophobic Bonds b. Hetero-oligomers – with several distinct
à Formed by the interaction between subunits
nonpolar hydrophobic side chains. E.g. Hemoglobin – with 2 alpha and 2 beta
à Bonds cause nonpolar molecules to subunits. it is therefore hetero-oligomeric protein
adhere to one another.
à The major driving force in protein
folding
à Spontaneous folded state of
globular protein reflects the balance
between opposing energetics of
hydrogen bonding between hydrophilic
R and aqueous environment and
repulsion from aqueous environment
by hydrophobic R group
à Hydrophobicity of certain R groups
tend to drive them away from aqueous
environment
2. Electrostatic/Ionic bonds Figure 26. Quaternary Structure
à Attractive forces between two
opposite charges or repulsion between D. PROTEIN FOLDING
two like charges.
à Mainly three types: • Involves the packing of amino acids to assume its native
o charge - charge – refers to and functional conformation; makes use of disulfide
attraction between opposite bonds, covalent and non-covalent interactions
charge amino acids • Hydrophobic interactions drive protein folding
o charge- dipole – refers to • Proteins are conformationally dynamic molecules
interaction of ionized R à Renaturation – the ability of the protein to
groups with dipole of water refold if their confirmation has been disrupted
o dipole- dipole - interaction of • Native confirmation is favored, and regions of the native
R groups of amino acids structure persist even in the denatured state.
3. Van der Waals Forces à Denatured – a process in which a protein
• These are weak forces of attraction loses its natural confirmation by disruption of its
between polar and nonpolar structural order.
molecules. à Denaturation may be reversible or irreversible
• These forces are the summation of • Native confirmation of a protein is thermodynamically
various forms of energy resulting from favored
momentary random fluctuation in the • Folding is modular. Occurs in a stepwise process
distribution of electrons around any
atom which give rise to a transient

BCHM Amino Acids, Peptides and Proteins 7 of 8

STAGES
• First stage – short segments fold into secondary
structural units that provide local regions of organized
structure. Folding is now reduced to the selection of an
appropriate arrangement of this relatively small number of
secondary structural element.
• Second stage – the hydrophobic regions segregate into
the interior of the protein away from solvent, forming a
“molten globule”
à Molten globule – a partially folded
polypeptides in which modules of secondary
structure rearrange until mature conformation is
attained
• In general, each element of the secondary of super-
secondary structure, facilitates proper folding by directing
the folding process toward the native confirmation and
away from unproductive alternatives.
• For oligomeric proteins, individual proteins tend to fold
before they associate with other subunits.
• Chaperones
à Heat shock proteins
à Assist the covalent folding of unfolding and
the assembly or disassembly of other structures
à 2 types of Chaperones:
o Hsp70 – binds short sequences of
hydrophobic amino acids that energy
while a new polypeptide is being
synthesized, shielding them from
solvent
o Hsp60 – acts later in the folding
process. The central cavity of the
donut-shaped Hsp60 chaperone
provides a sheltered environment in
which a polypeptide can fold until all
hydrophobic regions are buried
interiorly, thus preempting any
tendency toward aggregation.
o Menkes syndrome – Insufficient copper
required by lysyl oxidase in the formation of
covalent cross-links w/c strengthen collagen
fibers
o Scurvy – Vit. C deficiency → inadequate
ascorbic acid → poor collagen synthesis
à Marfan Syndrome – overgrowth of long bones due
to mutations in gene encoding for fibrillin production
• Conditions involving protein conformation
à Prions – aggregates of insoluble proteins (misfolded) in
neural cells
o May trigger other proteins to fold abnormally
o Creutzfeldt-Jakob Disease – human variant of
mad cow disease
à Alzheimer’s Disease
o Aggregates of β-amyloid protein form plaques in
between neurons → disrupt cell function
o Tau protein detach from microtubules → tau proteins
fuse w/ other tau molecules → aggregation forms
tangles w/c disrupt synaptic communication
à Beta-Thalassemia – absence of chaperone in
incorporation of free hemoglobin into hemoglobin tetramer →
hemoglobin aggregation → cytotoxic effect to developing RBC
• Conditions involving genes
à Familial Hypercholesterolemia – mutation in gene
encoding for LDL receptor
à Carcinogenesis – disruption of basic protein structure due
to genetic mutations
REFERENCES
1) 2019, 2021, 2022 Trans
2) Murray, R. K. (2003). Harper's illustrated biochemistry. New York:
McGraw-Hill.
3) Voet, D., & Voet, J. G. (1995). Biochemistry. New York: J. Wiley &
Sons. Chicago

E. COMPLEX PROTEINS
• Proteins combined with another macromolecule
• Covalently bonded
• 2 types
1. Glycoproteins
• Proteins covalently conjugated with
carbohydrates
• Found in RBC surface, used in blood
typing
2. Lipoproteins
• Associated with storage and transport
of lipids
e.g. high density lipoprotein/ HDL
(good cholesterol) and low density
lipoprotein/LDL (bad cholesterol)

III. CLINICAL SIGNIFICANCE

• Conditions involving Fibrous Proteins
• Collagen – most abundant structural protein
à Too much collagen forms deposits within tissue
and may result to
o Pulmonary Fibrosis – scarring of lung
tissue; interferes with breathing
o Liver Fibrosis (Hepatic fibrosis) – may
lead to cirrhosis
à Insufficient collagen
o Ehlers-Danlos Syndrome – hyper-elastic
skin, hypermobility, hyper-extensive limbs
o Osteogenesis Imperfecta – brittle bones
due to type 1 collagen deficiency

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