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Proteins
Chapter 20
Table of Contents
20.1 Characteristics of Proteins
20.2 Amino Acids: The Building Blocks for Proteins
20.3 Essential Amino Acids
20.4 Chirality and Amino Acids
20.5 Acid–Base Properties of Amino Acids
20.6 Cysteine: A Chemically Unique Amino Acid
20.7 Peptides
20.8 Biochemically Important Small Peptides
20.9 General Structural Characteristics of Proteins
20.10 Primary Structure of Proteins
20.11 Secondary Structure of Proteins
20.12 Tertiary Structure of Proteins
20.13 Quaternary Structure of Proteins
20.14 Protein Hydrolysis
20.15 Protein Denaturation
20.16 Protein Classification Based on Shape
20.17 Protein Classification Based on Function
20.18 Glycoproteins
20.19 Lipoproteins
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Section 20.1
Characteristics of Proteins
• Amino acid - An organic compound that contains both an amino (-NH2) and
a carboxyl (-COOH) group attached to same carbon atom
– The position of carbon atom is Alpha (a)
– -NH2 group is attached at alpha (a) carbon atom.
– -COOH group is attached at alpha (a) carbon atom.
– R = side chain –vary in size, shape, charge, acidity, functional groups
present, hydrogen-bonding ability, and chemical reactivity.
– >700 amino acids are known
– Based on common “R” groups, there are 20 standard amino acids
Nomenclature
• Common names assigned to the amino acids are currently used.
• Three letter abbreviations - widely used for naming:
– First letter of amino acid name is compulsory and capitalized
followed by next two letters not capitalized except in the case of
Asparagine (Asn), Glutamine (Gln) and tryptophan (Trp).
• One-letter symbols - commonly used for comparing amino acid
sequences of proteins:
– Usually the first letter of the name
– When more than one amino acid has the same letter the most
abundant amino acid gets the 1st letter.
Practice Exercise
• Classify the following amino acids based on the polarity of their R-groups
Practice Exercise
• Classify the following amino acids based on the polarity of their R-groups
Non-polar
Non-polar
Polar Neutral
Polar Basic
Polar Acidic
• Since casein evidently supplies all the required amino acids in the correct
proportions needed for growth, it is called a complete protein.
• A complete protein contains all the essential amino acids in the proper amounts.
• An incomplete protein is low in one or more of the essential amino acids, usually
lysine, tryptophan, or methionine. Except for gelatin, proteins from animal sources
are complete, whereas proteins from vegetable sources are incomplete except soy
protein.
Practice Exercise
• Name the following amino acids with correct designation for
the enantiomer (chiral carbon is indicated by *).
A B C
COOH COOH COOH
*C H2N *C H
H 2N H H *C NH2
CH2 SH
CH3
OH
Practice Exercise
• Name the following amino acids with correct designation for
the enantiomer (chiral carbon is indicated by *).
A B C
COOH COOH COOH
*C H2N *C H
H 2N H H *C NH2
CH2 SH
CH3
OH
A = L-Isoleucine
B = D-Cysteine
C = L-Tyrosine
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Section 20.5
Acid–Base Properties of Amino Acids
• In pure form amino acids are white crystalline solids
• Most amino acids decompose before they melt
• Not very soluble in water
• Under physiological conditions exists as Zwitterions: An ion with +
(positive) and – (negative) charges on the same molecule with a net
zero charge
– Carboxyl groups give-up a proton to get negative charge
– Amino groups accept a proton to become positive
+
H H
H 3N CH C N CH C N CH C O-
Isomeric Peptides
• Peptides that contain the same amino acids but present
in different order are different molecules (constitutional
isomers) with different properties
– For example, two different dipeptides can be formed
between alanine and glycine
• The number of isomeric peptides possible increases
rapidly as the length of the peptide chain increases
Drill
• Write the structure of the tetrapeptide lys-ser-asp-ala at
the isoelectric point. Calculate its pI.
- partly responsible for triggering pain, - completely inactive, hence, the name
welt formation (as in scratches), bogus or false
movement of smooth muscle, and
lowering of blood pressure
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Sequencing a Protein
Enzymatic Hydrolysis
1) Exopeptidases – cleaves external peptide bonds
a) aminopeptidase – sequentially cleave peptide bonds beginning
at the N-terminal end
b) carboxypeptidase – sequentially cleave peptide bonds beginning
at the C-terminal end
2) Endopeptidases – cleaves internal peptide bonds
a) trypsin – cleaves peptide bonds at the carboxyl end of two
strongly basic aa’s : Arg & Lys
b) chymotrypsin – cleaves peptide bonds at the carboxyl end of the
three aromatic aa’s: Phe, Tyr, & Trp; Leu
c) pepsin – cleaves peptide bonds at the amino end of the three
aromatic aa’s: Phe, Tyr, & Trp; Ileu
• A. N-terminal end
b) Sanger’s method
2,4-dinitrofluorobenzene (DNFB)
binds to the N-terminal amino group of
the polypeptide. The resultant
dinitrophenyl-amino acid or DNP-aa
can be separated from the other
amino acids because it is more
soluble in nonpolar solvents
• B. C-terminal end
Hydrazine method
hydrazine reacts with all amino
acids whose carboxyl group is
bound in peptide linkage, creating
amino acyl hydrazides. Only the C-
terminal amino acid is spared
Drills
1. Write the peptides generated from chymotrypsin, trypsin, and pepsin
digestion of
Ala-His-Tyr-Pro-Trp-Arg-Ileu-Phe-Glu-Lys-Cys
• The peptide linkages are essentially planar thus allows only two possible
arrangements for the peptide backbone for the following reasons:
– For two amino acids linked through a peptide bond six atoms lie in the same
plane
– The planar peptide linkage structure has considerable rigidity, therefore rotation
of groups about the C–N bond is hindered
– Cis–trans isomerism is possible about C–N bond.
– The trans isomer is the preferred orientation
The only bond responsible for the 2o structure of proteins is H-bonding
between peptide bonds, the – C = O of one peptide group and the – N – H
of another peptide linkage farther along the backbone.
The two most common types : alpha-helix (a-helix) and the beta-pleated sheet
(b-pleated sheet).
Alpha-helix (α-helix)
• A single protein chain adopts a
shape that resembles a coiled
spring (helix):
– H-bonding between amino
acids with in the same
chain –intramolecular H-
bonding
– Coiled helical spring
– R-groups stay outside of
the helix -- not enough
room for them to stay
inside
– The helix is so tightly
wound that the space in
the center is too small for
solvent molecules to enter
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Section 20.11
Secondary Structure of Proteins
Beta-Pleated Sheets
• Completely extended
protein chain segments in
same or different molecules
governed by intermolecular
or intramolecular H-bonding
• H-bonding between different
parts of a single chain –
intramolecular H-bonding
• Side chains below or above
the axis
• “U-turn” structure – most
frequently encountered
Beta-Pleated Sheets
• Completely extended
protein chain segments in
same or different molecules
• H-bonding between different
chains – intermolecular H-
bonding
a) parallel – chains run in
the same direction
b) antiparallel – chains run
in opposite direction;
more stable because
of fully collinear H-
bonds
Immunoglobulins
• Glycoproteins produced as a protective response to the invasion of
microorganisms or foreign molecules - antibodies against antigens.
• Immunoglobulin bonding to an antigen via variable region of an
immunoglobulin occurs through hydrophobic interactions, dipole –
dipole interactions, and hydrogen bonds.
• Carbohydrate molecules attached to the heavy chains aid in
determining the destinations of immunoglobulins in the tissues