Chemistry Chapter 22
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1 hemistry 2100 hapter 22
2 Proteins Proteins serve many functions, including the following. 1. Structure: ollagen and keratin are the chief constituents of skin, bone, hair, and nails. 2. atalysts: Virtually all reactions in living systems are catalyzed by proteins called enzymes. 3. Movement: Muscles are made up of proteins called myosin and actin. 4. Transport: emoglobin transports oxygen from the lungs to cells; other proteins transport molecules across cell membranes. 5. ormones: Many hormones are proteins, among them insulin, oxytocin, and human growth hormone.
3 Proteins 6. Protection: Blood clotting involves the protein fibrinogen; the body used proteins called antibodies to fight disease. 7. Storage: asein in milk and ovalbumin in eggs store nutrients for newborn infants and birds. Ferritin, a protein in the liver, stores iron. 8. Regulation: ertain proteins not only control the expression of genes, but also control when gene expression takes place. Proteins are divided into two types: Fibrous proteins Globular proteins
4 2 R nonpolar polar / neutral acidic / basic
5 hirality of α-amino Acids With the exception of glycine, all proteinderived amino acids have at least one stereocenter (the α-carbon) and are chiral. The vast majority of α-amino acids have the L- configuration at the α-carbon D-Alanine L-Alanine (Fischer projections)
6 2 R nonpolar polar / neutral acidic / basic
7 Protein-Derived α-amino Acids onpolar side chains (at p 7.0) Alanine (Ala, A) Phenylalanine (Phe, F) Glycine (Gly, G) - Proline (Pro, P) S Isoleucine (Ile, I) Leucine (Leu, L) Methionine (Met, M) Tryptophan (Trp, W) Valine (Val, V)
8 Protein-Derived α-amino Acids Polar side chains (at p 7.0) Asparagine (Asn, ) S ysteine (ys, ) Glutamine (Gln, Q) Serine (Ser, S) Tyrosine (Tyr, Y) Threonine (Thr, T)
9 Protein-Derived α-amino Acids Acidic and basic side chains (at p 7.0) Aspartic acid (Asp, D) Glutamic acid (Glu, E) Arginine (Arg, R) istidine (is, ) Lysine (Lys, K)
10 essential amino acids Leu, Ile, Lys, Met, Phe, Thr, Trp, Val, is ( Arg, Tyr, ys )
11 R R R zwitterion
12 Ionization vs. p The net charge on an amino acid depends on the p of the solution in which it is dissolved. If we dissolve an amino acid in water, it is present in the aqueous solution as its zwitterion. If we add a strong acid such as l to bring the p of the solution to 0.0, the strong acid donates a proton to the - - of the amino acid turning the zwitterion into a positive ion R R + 2
13 Ionization vs. p If we add a strong base such as a to the solution and bring its p to 14, a proton is transferred from the 3 + group to the base turning the zwitterion into a negative ion R To summarize: R R R R
14 Problem: alculate the net charge of lysine at p = 3, 7, 11. Estimate pi for lysine
15 p = 7
16 ( ) p = 7
17 ( ) (+) p = 7
18 ( ) (+) p = 7 (+)
19 ( ) 2 (+) (+) p = 7
20 ( ) 2 (+) (+) p = 3 p = 7
21 ( ) (+) 2 (+) 2 (+) (+) p = 3 p = 7
22 ( ) (+) 2 (+) 2 2 (+) (+) p = 3 p = 7 p = 11
23 ( ) ( ) (+) 2 (+) 2 2 (+) (+) p = 3 p = 7 p = 11
24 Isoelectric Point (pi) Isoelectric point, pi: The p at which the majority of molecules of a compound in solution have no net charge. onpolar & polar side chains alanine asparagine cysteine glutamine glycine isoleucine leucine methionine phenylalanine proline serine threonine tyrosine tryptophan valine pi Acidic Side hains aspartic acid glutamic acid Basic Side hains arginine histidine lysine pi pi
25 Problem: Predict the electrophoresis behavior at p 6.0 of a mixture of alanine (pi 6.0), aspartic acid (pi 2.8) and lysine (pi 9.7)
26 Problem: Predict the electrophoresis behavior at p 6.0 of a mixture of alanine (pi 6.0), aspartic acid (pi 2.8) and lysine (pi 9.7)
27 Problem: Predict the electrophoresis behavior at p 6.0 of a mixture of alanine (pi 6.0), aspartic acid (pi 2.8) and lysine (pi 9.7)
28 Problem: Predict the electrophoresis behavior at p 6.0 of a mixture of alanine (pi 6.0), aspartic acid (pi 2.8) and lysine (pi 9.7) Lys Ala Asp
29 Peptide Bonds (-) 2 R R' R R'
30 Peptide Bonds (-) 2 R R' R R'
31 Peptide Bonds (-) 2 R R' R R'
32 Peptide Bonds (-) 2 R R' R R'
33 Peptide Bonds (-) 2 R R' R R'
34 R' R" α α α α α R R" R" "
35 R' R" α α α α α R R" R" "
36 R' R" α α α α α R R" R" "
37 R' R" α α α α α R R" R" "
38 R' R" α α α α α R R" R" "
39 (-terminus) (+) 2 (+) ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) (+) ( )
40 (-terminus) (+) 2 (+) ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) (+) ( )
41 (-terminus) (+) 2 (+) ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) (+) ( )
42 (-terminus) (+) 2 (+) ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) (+) ( )
43 (-terminus) (+) 2 (+) ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) (+) ( )
44 (-terminus) 2 ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) ( ) p = 7
45 (-terminus) (+) 2 (+) ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) (+) ( ) p = 7
46 (-terminus) (+) 2 (+) ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) (+) ( ) p = 3
47 (-terminus) (+) 2 (+) ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) (+) ( ) p = 3
48 (-terminus) 2 ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) ( ) p = 11
49 (-terminus) 2 ( ) ( 2 ) S 3 2 ( 2 ) 3 2 lysylserylmethionylaspartylarginine [Lys Ser Met Asp Arg] (-terminus) ( ) p = 11
50 Lys œ Ser œ Met œ Asp œ Arg or - Arg Asp Lys Met Ser (5!) = 120 combinations (20!) = eicosapeptides (20 5 ) = possible pentapeptide
51 Lys œ Ser œ Met œ Asp œ Arg or - Arg Asp Lys Met Ser (5!) = 120 combinations (20!) = eicosapeptides (20 5 ) = possible pentapeptide
52 Lys œ Ser œ Met œ Asp œ Arg or - Arg Asp Lys Met Ser (5!) = 120 combinations (20!) = eicosapeptides (20 5 ) = possible pentapeptide
53 Lys œ Ser œ Met œ Asp œ Arg or - Arg Asp Lys Met Ser (5!) = 120 combinations (20!) = eicosapeptides (20 5 ) = possible pentapeptide
54 Lys œ Ser œ Met œ Asp œ Arg or - Arg Asp Lys Met Ser (5!) = 120 combinations (20!) = eicosapeptides (20 5 ) = possible pentapeptide
55 Lys œ Ser œ Met œ Asp œ Arg or - Arg Asp Lys Met Ser (5!) = 120 combinations (20!) = eicosapeptides (20 5 ) = possible pentapeptides
56 S S 2 ys ys Pro Leu Gly 2 Tyr Ile Gln Asn oxytocin S S 2 ys ys Pro Arg Gly 2 Tyr Phe Gln Asn vasopressin
57 Enkephalins 3 Morphine Tyr Gly Gly Phe Met Tyr Gly Gly Phe Leu Methionine Leucine enkephalin
58 Insulin S S Gly Ile Val Glu Gln ys ys Thr Ser Ile ys Ser Leu Tyr Gln Leu Glu Asn Tyr ys Asn S S S Phe Val Asn Gln is Leu ys Gly Ser is Leu Val Glu Ala Leu Tyr Leu Val ys Gly Glu Arg Gly Phe Phe Tyr Thr Pro Lys Thr S
59 Structure of Proteins
60 R R' R" R" R" " R
61 R R' R" R" R" " R
62 R R' R" R" R" " R
63 R R' R" R" R" " R
64 Secondary Structure: The α-elix
65 β-pleated Sheet
66 Random oil
67 β-pleated sheet α-helix α-helix β-pleated sheet
68 Protein Tertiary Structure
69 β-pleated sheet α-helix α-helix β-pleated sheet
70 β-pleated sheet α-helix salt bridge α-helix β-pleated sheet
71 β-pleated sheet α-helix salt bridge α-helix 2 hydrogen bond 2 β-pleated sheet
72 β-pleated sheet α-helix hydrogen bond salt bridge α-helix 2 hydrogen bond 2 β-pleated sheet
73 hydrophilic interaction to water β-pleated sheet α-helix hydrogen bond 2 salt bridge α-helix 2 hydrogen bond 2 β-pleated sheet
74 hydrophilic interaction to water β-pleated sheet α-helix hydrogen bond hydrophobic interaction 2 salt bridge α-helix 2 hydrogen bond 2 β-pleated sheet
75 hydrophilic interaction to water β-pleated sheet α-helix hydrogen bond hydrophobic interaction salt bridge α-helix 2 hydrogen bond 2 β-pleated sheet
76 hydrophilic interaction to water β-pleated sheet α-helix hydrogen bond hydrophobic interaction salt bridge S S disulfide bond S S α-helix 2 hydrogen bond 2 β-pleated sheet
77 Protein Quaternary Structure
78 emoglobin S 8 Fe 4 (MW 64,450)
79 Sickle-ell Anemia
80 Sequence Varies: Ask 23andMe
81 Proteins
82 Denaturation
83 Denaturation also known as ooking
84 Misfolding Diseases
85 Mutation Impairs Proper Folding ystic Fibrosis Sickle ell Anemia
86 ontagious Misfolding: Prions
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