AMINO ACIDS. CHAPTER 19: Proteins. Page 19-1
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1 APTE 19: Proteins Identify the characteristic parts of an α- amino acid and understand how group character affects amino acid and protein properties Describe important chemical reactions of amino acids (peptide formation, disulfide bridge formation) Explain how 1, 2, 3, and 4 structure arise from the basic sequence of amino acids in a protein haracterize proteins in terms of shape, composition, and function AMI AIDS Table 18.1, p 529 L FIGUATI α 2 SIDE AI 20 different amino acids make up proteins 2 amino acids are acidic: ends in 3 amino acids are basic: ends in Balance are neutral PTEIS AE PLYMES F α-ami AIDS 10 amino acids are essential: must be present in food Arginine* (Arg, ) Methionine(Met, M) istidine* (is, ) Phenylalanine (Phe, F) Isoleucine (Ile, I) Threonine (Thr, T) Leucine (Leu, L) Tryptophan (Trp, W) D-Proline L-Proline D-Proline (rotated) Lysine (Lys, K) * Infants and growing children Valine (Val, V) Amino acids can act as both acid and base 3 + LWE p + ~ p p 3 ( ( = acidic) acidic) ~ p p 6 ( ( = neutral) ~ p p 9 ( ( = basic) basic) ZWITTEI o net charge ISELETI PIT IGE p (p = pi) Physiological p is near neutral for blood for other fluids Side chains of acidic and basic amino acids are ionized at physiological p: Asp p < 1 p = pi = 2.77 p = 7 p > 12 Lys 2 ( 2 ) ( 2 ) ( 2 ) 4 2 ( 2 ) 4 2 p < 1 p = 7 p = pi = 9.74 p > 12 Page 19-1
2 19.3 EATIS of AMI AIDS YSTEIE XIDATI 2 S 2 2 YSTEIE [] [] 2 S S YSTIE Formation of of DISULFIDE BIDGE PEPTIDE FMATI = PEPTIDE BD -TEMIAL ESIDUE -TEMIAL ESIDUE PTEI Polyamide of of L-α-amino acid residues º of Amino Acids Linked ame AMI AID DIPEPTIDE TIPEPTIDE PLYPEPTIDE PTEI 19.5 PTEI AATEISTIS Acid-Base Properties Size PTEI Insulin ytochrome c Growth hormone emoglobin exokinase Myosin MW (amu) ESIDUES 6, , , , , , Types and distribution of groups in a protein determine its characteristic isoelectric point At p values above or below pi, protein molecules repel each other and remain dispersed At pi, protein molecules tend to clump together and precipitate from solution p pi Page 19-2
3 Function ATALYSIS Enzymes STUTUE Fibrous proteins STAGE asein, ovalbumin PTETI Immunoglobins PESS EGULATI ormones SIGAL TASMISS eural receptor proteins MVEMET ontractile proteins TASPT emoglobin, lipoproteins lassification BY SAPE FIBUS» Insoluble in 2» Structural functions GLBULA» Soluble in 2» on-structural functions BY MPSITI SIMPLE Amino acid polymer JUGATED Amino acid polymer + non-protein substances ME MM onjugated proteins require non-protein PSTETI GUPS to function LASS Lipoproteins Glycoproteins Phosphoproteins Metalloproteins emoproteins PSTETI GUP lipids EX: emoglobin carbohydrates phosphate metal ions heme EXAMPLE serum liporoteins gamma globulin casein alcohol dehydrogenase cytochromes EME GUP EME GUP 19.6 PIMAY STUTUE ALAIE (Ala) - 2 SEIE (Ser) ALAYLSEIE (Ala-Ser) MPAE: SEYLALAIE (Ser-Ala) Different residue sequence = different properties 3 + BAKBE PIMAY STUTUE The sequence of of covalently-linked amino acids - Example: EMGLBI β-ai ( b ): ormal -Thr-Pro-Glu-Lys-Ala Abnormal -Thr-Pro-Val-Lys-Ala 2/molecule (each parent contributes to the formation of 1): + = MAL + A A + A = SIKLE TAIT malaria resistance = SIKLE ELL AEMIA Page 19-3
![19.7 SEDAY STUTUE ormal emoglobin Abnormal emoglobin: @ low [ 2 ], clumps to form long helical fibers LGS APILLAIES epeating, oriented](/docs-images/72/67527241/images/4-0.jpg "arrangement of of protein chain due to to backbone -bonding α-elix Bundled α-helices give mechanical strength to to fibrous proteins in in")
4 19.7 SEDAY STUTUE ormal emoglobin Abnormal low [ 2 ], clumps to form long helical fibers LGS APILLAIES epeating, oriented arrangement of of protein chain due to to backbone -bonding α-elix Bundled α-helices give mechanical strength to to fibrous proteins in in muscle myosin β-pleated SEET Bundled β-pleated sheets give mechanical strength to to fibrous proteins in in silk fibroin β-bael β-strands β-barrels bind and transport hydrophobic molecules such as as vitamin A (retinol) β-tu β-turns allow proteins to to reverse the peptide chain direction Page 19-4
5 19.8 TETIAY STUTUE ydrogen Bonding Salt Bridge At physiological p (~7), side chains affect the physical and chemical environment along the petide chain: BASE Ion-ion 2 2 S 3 EUTAL, PLA Dispersion forces EUTAL, PLA -bonding AID Ion-ion EUTAL, PLA Dispersion forces S S Disulfide Bridge ydrophobic Interaction Folding of of protein chain due to to side-chain interactions QUATEAY STUTUE emoglobin ombination of of 2 or or more globular protein subunits into a larger structure PI PTEI (~250 bases): α-helices strand of β-pleated sheet YDLYSIS & DEATUATI YDLYSIS eating a peptide or in the presence of acid or base causes it to break down into smaller fragments smaller peptides or amino acids BEIG STUTUE TLS FUTI IFETIUS (speculative) Asp Arg Val Tyr Ile is Pro Phe 2 protease Asp Arg Val Tyr Ile is Pro Phe 2 peptidase Asp Arg Val Tyr Ile is Pro Phe Page 19-5
6 DEATUATI SALT BIDGES YDGE BDS EAT or UV LIGT X X MEAIAL AGITATI DISULFIDE BIDGE Destruction or or disruption of of secondary or or higher-order structure YDPBI ITEATIS DETEGETS X X X PLA SLVETS X STG AID or BASE X X EAVY METAL IS X X X DEATUATI LEADS T LSS F FUTI Page 19-6
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