Organic Chemistry, 6th Edition
L. G. Wade, Jr.
Amino Acidos,
Peptidos, y Proteinas
Jo Blackburn
Richland College, Dallas, TX
Dallas County Community College District
2006, Prentice Hall
Proteinas
• Biopolymers of -amino acids.
• Amino acids are joined by peptide bond.
• Variety of functions:
structure
enzymes
transport
protection
hormones
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Chapter 24
2
Zwitterion
• Amino acid exists as a dipolar ion.
• -COOH loses H+, -NH2 gains H+.
•
Actual structure depends on pH.
Chapter 24
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3
Properties of Amino Acids
• High melting points, over 200C.
• More soluble in water than in ether.
• Larger dipole moments than simple
acids or simple amines.
• Less acidic than most carboxylic acids,
less basic than most amines.
O
pKa = 10
_
+
H3N CH C O
pKb = 12
R
Chapter 24
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4
Isoelectric Point
• pH at which amino acids exist as the
zwitterion (neutral).
• Depends on structure of the side chain.
• Acidic amino acids, isoelectric pH ~3.
• Basic amino acids, isoelectric pH ~9.
• Neutral amino acids, isoelectric pH is
slightly acidic, 5-6.
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5
Reductive Amination
• This method for synthesizing amino acids is
biomimetic, mimics the biological process.
• React an -ketoacid with ammonia, then
reduce the imine with H2/Pd.
• Racemic mixture is obtained.
• Use enzyme catalyst to obtain pure L form.
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Chapter 24
6
Transamination
• Biosynthesis of other amino acids from
L-glutamic acid
• Only one enantiomer produced.
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Chapter 24
7
Peptide Bond Formation
• The amino group of one molecule condenses
with the acid group of another.
• Polypeptides usually have molecular weight
less than 5000.
• Protein molecular weight 6000-40,000,000.
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Chapter 24
8
Bradykinin
• An oligopeptide, four to ten amino acids.
• Peptide structures are drawn with the Nterminal end at the left.
• Peptides are named from left to right:
arginylprolylprolyl……arginine.
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Chapter 24
9
Disulfide Linkages
Cysteine can form disulfide bridges.
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Chapter 24
10
Peptide Structure
Determination
• Cleavage of disulfide linkages
• Determination of amino acid
composition
• Sequencing from the N terminus
• C-Terminal residue analysis
• Partial hydrolysis
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Chapter 24
11
Disulfide Cleavage
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Chapter 24
12
Amino Acid Composition
• Separate the individual peptide chains.
• Boil with 6 M HCl for 24 hours.
• Separate in an amino acid analyzer.
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Chapter 24
13
Sequencing from
the N Terminus
• Edman degradation: reaction with
phenyl isothiocyanate followed by
hydrolysis removes the N terminus
amino acid.
• The phenylthiohydantoin derivative is
identified by chromatography.
• Use for peptides with < 30 amino acids.
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Chapter 24
14
Solid Phase
Peptide Synthesis
• Growing chain, built from C to N terminus,
is attached to polystyrene beads.
• Intermediates do not have to be purified.
• Excess reagents are washed away with a
solvent rinse.
• Process can be automated.
• Larger peptides can be constructed.
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Chapter 24
15
Classification
of Proteins
• Simple: hydrolyze to amino acids only.
• Conjugated: bonded to a nonprotein
group, such as sugar, nucleic acid, or
lipid.
• Fibrous: long, stringy filaments, insoluble
in water, function as structure.
• Globular: folded into spherical shape,
function as enzymes, hormones, or
transport proteins.
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Chapter 24
16
Levels of
Protein Structure
• Primary: the sequence of the amino
acids in the chain and the disulfide links.
• Secondary: structure formed by
hydrogen bonding. Examples are helix and pleated sheet.
• Tertiary: complete 3-D conformation.
• Quaternary: association of two or more
peptide chains to form protein.
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Chapter 24
17
Alpha Helix
Each carbonyl oxygen can hydrogen
bond with an N-H hydrogen on the next
turn of the coil.
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Chapter 24
18
Pleated Sheet
Each carbonyl oxygen hydrogen
bonds with an N-H hydrogen on an
adjacent peptide chain.
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Chapter 24
19
Summary of Structure
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Chapter 24
20
Desnaturalizacion
• Disruption de la estructura normal de
una proteina, perdiendo actividad
biologica.
• Usualmente causado por cambios en
calor y pH.
• Usualmente Irreversible cuando se
cocina un huevo.
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Chapter 24
21