Nonpolar Aliphatic Amino Acids CH3 CH3 H CH3 -CH3 HO cooe Cooe H,N Isoleucine (le; I) HạN coo H,N Alanıne (Ala; A) H3N Glyclne (Gly; G) Valline (Val; V) Leudine (Leu; L) Nonpolar Aromatic Amino Acids но Nonpolar Amino Acids CH3 HN HgN H,N HN COo Co Prolline (Pro; P) Methlonine (Met; M) Phenylalanlne (Phe; F) Tyroslne (Tyr; Y) Tryptophan (Trp; w) Polar Amino Acids NH2 - NH2 но HS Но CH COoe cooe C00 e co0e Serine (Ser; S) Cystelne (Cys; C) Threonine (Thr; T) Asparaglne (Asn; N) Glutamine (Gin; Q) Positively Charged Polar Amino Acids Negatively Charged Polar Amino Acids H,N NH2 HN HN: e COoe cooe coo cooe HIstidine (Hls; H) Lysine (Lys; K) Arginine (Arg; R) Aspartic Acld (Asp; D) Glutamlc Acld (Glu; E) A FIGURE 5.3 The 20 common amino acids found in proteins. The chemical structures of the 20 common a-amino acids that are incorporated into proteins are shown and arranged here in the order in which they are discussed in the text. The "side chain" or "R group" of each amino acid is highlighted in green. Below each amino acid are its name, its three-letter abbreviation, and its one-letter abbreviation. TABLE 5.1 Properties of the common amino acids found in proteins Abbreviations: 1- pK, of a-COOH and 3-letter codes pKg of a-NHj Group pKg of lonizing Side Chain Residue Mass (daltons) Occurrence in Name Group Proteins (mol %) Alanine А, Ala 2.3 9.7 71.08 8.7 Arginine R, Arg 2.2 9.0 12.5 156.20 5.0 Asparagine Aspartic acid N, Asn 2.0 8.8 114.11 4.2 D, Asp 2.1 9.8 3.9 115.09 5.9 C, Cys Q, Gln Cysteine 1.8 10.8 8.3 103.14 1.3 Glutamine 2.2 9.1 128.14 3.7 Glutamic acid E, Glu 2.2 9.7 4.2 129.12 6.6 Glycine G, Gly 2.3 9.6 57.06 7.9 Histidine H, His 1.8 9.2 6.0 137.15 2.4 I, lle L, Leu Isoleucine 2.4 9.7 113.17 5.5 Leucine 2.4 9.6 113.17 8.9 К, Lys М, Met F, Phe P, Pro S, Ser Lysine 2.2 9.0 10.0 128.18 5.5 Methionine 2.3 9.2 131.21 2.0 Phenylalanine 1.8 9.1 147.18 4.0 Proline 2.0 10.6 97.12 4.7 Serine 2.2 9.2 87.08 5.8 Threonine T, Thr 2.6 10.4 101.11 5.6 W, Trp Y, Tyr V, Val Tryptophan 2.4 9.4 186.21 1.5 Tyrosine 2.2 9.1 10.1 163.18 3.5 Valine 2.3 9.6 99.14 7.2
Nonpolar Aliphatic Amino Acids CH3 CH3 H CH3 -CH3 HO cooe Cooe H,N Isoleucine (le; I) HạN coo H,N Alanıne (Ala; A) H3N Glyclne (Gly; G) Valline (Val; V) Leudine (Leu; L) Nonpolar Aromatic Amino Acids но Nonpolar Amino Acids CH3 HN HgN H,N HN COo Co Prolline (Pro; P) Methlonine (Met; M) Phenylalanlne (Phe; F) Tyroslne (Tyr; Y) Tryptophan (Trp; w) Polar Amino Acids NH2 - NH2 но HS Но CH COoe cooe C00 e co0e Serine (Ser; S) Cystelne (Cys; C) Threonine (Thr; T) Asparaglne (Asn; N) Glutamine (Gin; Q) Positively Charged Polar Amino Acids Negatively Charged Polar Amino Acids H,N NH2 HN HN: e COoe cooe coo cooe HIstidine (Hls; H) Lysine (Lys; K) Arginine (Arg; R) Aspartic Acld (Asp; D) Glutamlc Acld (Glu; E) A FIGURE 5.3 The 20 common amino acids found in proteins. The chemical structures of the 20 common a-amino acids that are incorporated into proteins are shown and arranged here in the order in which they are discussed in the text. The "side chain" or "R group" of each amino acid is highlighted in green. Below each amino acid are its name, its three-letter abbreviation, and its one-letter abbreviation. TABLE 5.1 Properties of the common amino acids found in proteins Abbreviations: 1- pK, of a-COOH and 3-letter codes pKg of a-NHj Group pKg of lonizing Side Chain Residue Mass (daltons) Occurrence in Name Group Proteins (mol %) Alanine А, Ala 2.3 9.7 71.08 8.7 Arginine R, Arg 2.2 9.0 12.5 156.20 5.0 Asparagine Aspartic acid N, Asn 2.0 8.8 114.11 4.2 D, Asp 2.1 9.8 3.9 115.09 5.9 C, Cys Q, Gln Cysteine 1.8 10.8 8.3 103.14 1.3 Glutamine 2.2 9.1 128.14 3.7 Glutamic acid E, Glu 2.2 9.7 4.2 129.12 6.6 Glycine G, Gly 2.3 9.6 57.06 7.9 Histidine H, His 1.8 9.2 6.0 137.15 2.4 I, lle L, Leu Isoleucine 2.4 9.7 113.17 5.5 Leucine 2.4 9.6 113.17 8.9 К, Lys М, Met F, Phe P, Pro S, Ser Lysine 2.2 9.0 10.0 128.18 5.5 Methionine 2.3 9.2 131.21 2.0 Phenylalanine 1.8 9.1 147.18 4.0 Proline 2.0 10.6 97.12 4.7 Serine 2.2 9.2 87.08 5.8 Threonine T, Thr 2.6 10.4 101.11 5.6 W, Trp Y, Tyr V, Val Tryptophan 2.4 9.4 186.21 1.5 Tyrosine 2.2 9.1 10.1 163.18 3.5 Valine 2.3 9.6 99.14 7.2
Human Heredity: Principles and Issues (MindTap Course List)
11th Edition
ISBN:9781305251052
Author:Michael Cummings
Publisher:Michael Cummings
Chapter10: From Proteins To Phenotypes
Section: Chapter Questions
Problem 14QP: If phenylalanine was not an essential amino acid, would diet therapy (the elimination of...
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What is the optimum pH to separate a mixture of lysine, arginine, and
cysteine using electrophoresis? Draw the structures of the three amino acids
in the protonation state that would predominate at the pH you have chosen.
(as shown) For each amino acid, indicate the net charge at the chosen pH as well as the direction of migration and relative mobility in the electric field.
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