amino acids proteins, and enzymes
DESCRIPTION
Types of Proteins Amino Acids The Peptide Bond. Amino Acids Proteins, and Enzymes. TypeExamples Structuraltendons, cartilage, hair, nails Contractilemuscles Transporthemoglobin Storagemilk Hormonalinsulin, growth hormone Enzymecatalyzes reactions in cells - PowerPoint PPT PresentationTRANSCRIPT
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Amino Acids Proteins, and Amino Acids Proteins, and EnzymesEnzymes
Types of ProteinsAmino Acids
The Peptide Bond
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Types of ProteinsTypes of ProteinsType Examples
Structural tendons, cartilage, hair, nails
Contractile musclesTransport hemoglobinStorage milkHormonal insulin, growth hormoneEnzyme catalyzes reactions in cellsProtection immune response
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Amino AcidsAmino AcidsBuilding blocks of proteinsCarboxylic acid groupAmino groupSide group R gives unique
characteristics
R side chain IH2H—C —COOH I H
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Examples of Amino AcidsExamples of Amino Acids H IH2N—C —COOH I H glycine CH3 IH2N—C —COOH I H alanine
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Types of Amino AcidsTypes of Amino AcidsNonpolar R = H, CH3, alkyl groups,
aromatic O
Polar llR = –CH2OH, –CH2SH, –CH2C–NH2, (polar groups with –O-, -SH, -N-)
Polar/Acidic R = –CH2COOH, or -COOH
Polar/ BasicR = –CH2CH2NH2
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Learning Check AA1Learning Check AA1Identify each as (1) polar or (2) nonpolar
A. NH2–CH2–COOH (Glycine)
CH3 | CH–OH
|B. NH2–CH–COOH (Serine)
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Solution AA1Solution AA1Identify each as (1) polar or (2) nonpolar
A.(2) NH2–CH2–COOH (Glycine)
CH3 | CH–OH |B. (1) NH2–CH–COOH (Serine)
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Essential Amino AcidsEssential Amino Acids10 amino acids not synthesized by the
bodyarg, his, ile, leu, lys, met, phe, thr, trp,
valMust obtain from the dietAll in dairy products 1 or more missing in grains
and vegetables
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Amino Acids as Acids and BasesAmino Acids as Acids and BasesIonization of the –NH2 and the –COOH
groupZwitterion has both a + and – chargeZwitterion is neutral overall
+NH2–CH2–COOH H3N–CH2–COO–
glycine Zwitterion of glycine
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pH and ionizationpH and ionization
H+ OH–
+ +H3N–CH2–COOH H3N–CH2–COO– H2N–CH2–
COO– Positive ion zwitterion Negative
ionLow pH neutral pH High pH
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The Peptide BondThe Peptide BondAmide bond formed by the –COOH of an amino acid and the –NH2 of the next amino acid O CH3
+ | | + |NH3–CH2–COH + H3N–CH–COO– O CH3
+ | | | NH3–CH2–C – N–CH–COO– | peptide bond H
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PeptidesPeptidesAmino acids linked by amide (peptide)
bonds
Gly Lys Phe Arg Ser
H2N-end COOH-end
Peptide bonds
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Learning Check AA3Learning Check AA3
What are the possible tripeptides formed from one each of leucine, glycine, and alanine?
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Solution AA3Solution AA3Tripeptides possible from one each of leucine, glycine, and alanine
Leu-Gly-AlaLeu-Ala-GlyAla-Leu-GlyAla-Gly-LeuGly-Ala-LeuGly-Leu-Ala
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Amino Acids, Proteins, and Amino Acids, Proteins, and EnzymesEnzymes
Primary and Secondary StructureTertiary and Quaternary Structure
Protein Hydrolysis and Denaturation
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Primary Structure of ProteinsPrimary Structure of ProteinsThe particular sequence of amino acids that is the backbone of a peptide chain or protein
H3N CHCH3
CO
NH
CH CO
NH
CH CO
NH
CH C O-OCH
CH CH3
CH3
CH2
SHCH2
CH2
SCH3
+
Ala-Leu-Cys-Met
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Secondary Structure – Alpha Secondary Structure – Alpha HelixHelix
Three-dimensional arrangement of amino acids with the polypeptide chain in a corkscrew shape
Held by H bonds between the H of –N-H group and the –O of C=O of the fourth amino acid along the chain
Looks like a coiled “telephone cord”
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Secondary Structure – Beta Secondary Structure – Beta Pleated SheetPleated Sheet
Polypeptide chains are arranged side by side
Hydrogen bonds form between chains
R groups of extend above and below the sheet
Typical of fibrous proteins such as silk
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Secondary Structure – Triple Secondary Structure – Triple HelixHelix
Three polypeptide chains woven together
Glycine, proline, hydroxy proline and hydroxylysine
H bonding between –OH groups gives a strong structure
Typical of collagen, connective tissue, skin, tendons, and cartilage
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Learning Check P1Learning Check P1Indicate the type of structure as(1) primary (2) alpha helix(3) beta pleated sheet (4) triple helix
A. Polypeptide chain held side by side by H bonds
B. Sequence of amino acids in a polypeptide chain
C. Corkscrew shape with H bonds between amino acids
D. Three peptide chains woven like a rope
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Solution P1Solution P1Indicate the type of structure as(1) primary (2) alpha helix(3) beta pleated sheet (4) triple helix
A. 3 Polypeptide chain held side by side by H bonds
B. 1 Sequence of amino acids in a polypeptide chain
C. 2 Corkscrew shape with H bonds between amino acids
D. 4 Three peptide chains woven like a rope
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Tertiary StructureTertiary StructureSpecific overall shape of a proteinCross links between R groups of
amino acids in chaindisulfide –S–S–
+
ionic –COO– H3N–H bonds C=O HO– hydrophobic –CH3 H3C–
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Globular and Fibrous ProteinsGlobular and Fibrous Proteins
Globular proteins Fibrous proteins
“spherical” shape long, thin fibers
Insulin HairHemoglobin WoolEnzymes SkinAntibodies Nails
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Quaternary StructureQuaternary StructureProteins with two or more chains
Example is hemoglobin Carries oxygen in blood
Four polypeptide chainsEach chain has a haem group to
bind oxygen
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Learning Check P3Learning Check P3Identify the level of protein structure1. Primary 2. Secondary3. Tertiary 4. Quaternary
A. Beta pleated sheetB. Order of amino acids in a proteinC. A protein with two or more peptide
chainsD. The shape of a globular proteinE. Disulfide bonds between R groups
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Solution P3Solution P3Identify the level of protein structure1. Primary 2. Secondary3. Tertiary 4. Quaternary
A. 2 Beta pleated sheetB. 1 Order of amino acids in a proteinC. 4 A protein with two or more peptide chainsD. 3 The shape of a globular proteinE. 3 Disulfide bonds between R groups
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Protein HydrolysisProtein HydrolysisBreak down of peptide
bonds Requires acid or base and
heatGives smaller peptides and
amino acids Similar to digestion of
proteins using enzymesOccurs in cells to provide
amino acids to synthesize other proteins and tissues
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Hydrolysis of a DipeptideHydrolysis of a Dipeptide
H3N CHCH3
CO
NH
CH COCH2
OH
OH
+
H3N CHCH3
COHO
+ CH COCH2
OH
OHH3N
H2O, H+
++
heat
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DenaturationDenaturationDisruption of secondary, tertiary and quaternary protein structure byheat/organics Break apart H bonds and disrupt hydrophobic attractions acids/ basesBreak H bonds between polar R groups andionic bondsheavy metal ions React with S-S bonds to form solidsagitation Stretches chains until bonds break
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Applications of DenaturationApplications of DenaturationHard boiling an eggWiping the skin with alcohol swab for
injectionCooking food to destroy E. coli.Heat used to cauterize blood vesselsAutoclave sterilizes instrumentsMilk is heated to make yoghurt
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Learning Check P4Learning Check P4What are the products of the complete hydrolysis of Ala-Ser-Val?
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Solution P4Solution P4The products of the complete hydrolysis of Ala-Ser-Val are
alanineserinevaline
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Learning Check P5Learning Check P5Tannic acid is used to form a scab on a burn. An egg becomes hard boiled when placed in hot water. What is similar about these two events?
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Solution P5Solution P5Acid and heat cause a denaturation of protein. They both break bonds in the secondary and tertiary structure of protein.
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DNADNA
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DNA RNADNA RNA
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DNA RNADNA RNA
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DNA RNADNA RNA
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DNA Backbone StructureDNA Backbone Structure Alternate phosphate and sugar (deoxyribose), phosphate ester bonds
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DNA Backbone StructureDNA Backbone Structure Alternate phosphate and sugar (deoxyribose), phosphate ester bonds
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DNA RNADNA RNA
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DNA Primary Structure SummaryDNA Primary Structure Summary
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DNA RNADNA RNA
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DNA Double HelixDNA Double Helix Base pairing by unique hydrogen bonds
C - G and A - T pairs
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DNA Double HelixDNA Double Helix Base pairing by unique hydrogen bonds
C - G and A - T pairs
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DNADNA
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DNA ReplicationDNA ReplicationComplementary base pairs form new strands.
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Types of RNATypes of RNAmRNA contains codons which code for amino acids.
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DNADNA
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Types of RNATypes of RNA rRNA - Ribosome - contains enzymes and keeps everything together
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Types of RNATypes of RNA tRNA - Transfer RNA carries amino acid and read codons
on m-RNA through its own anticodons.
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Types of RNATypes of RNA tRNA - Transfer RNA carries amino acid and read codons on m-RNA through its own
anticodons.