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Table 1. The most common endogenous opioid peptides produced in humans Рeptide Enkephalins Leu-enkephalin YGGFL Met-enkephalin YGGFM Metorphamide YGGFMRRV-NH2 Peptide E Peptide Sequence YGGFMRRVGRPEWWMDYQKRYGGFL Endorphins B-endorphin Y-endorphin a-endorphin YGGFMTSEKSQTPLVTLF KNAIIKNAYKKGE YGGFMTSEKSQTPLVTL YGGFMTSEKSQTPLVT Dynorphins Dynorphin A Dynorphin B Dynorphin1-8 YGGFLRRQ a-neoendorphin YGGFLRKYPK B-neoendorphin YGGFLRKYP YGGFLRRIRPKLKWDNQ YGGFLRRQFKWT 1. Endogenous opioids are peptides that are naturally produced in our bodies at low amounts and at specific times (see Table 1). These peptides bind to specific protein receptors in our nervous system that mediate pain signaling and reward. The chemical structure of an endogenous opioid peptide is shown below. но CHз S нн N. H2N HO н нн a) Determine the sequence of the peptide structure (in one-letter code): b) Based on the sequence and Table 1, what is the name of this peptide? c) How many of the alpha-carbons in the sequence are chiral (encircle one)? 1 2 3 4 5 6 d) How many peptide bonds are in the structure (encircle one)? 12 3 4 5 6 e) Identify all the peptide bonds by crossing out (place an X) at each peptide bond. f) How many ionizable functional groups are in the peptide (encircle one)? 1 2 3 4 5 6 g) Which amino acid in this peptide has a side chain that can form hydrogen bonds with water? Is this side-chain an H-bond donor, acceptor, or both? I ZI IZ о ZI I

Table 1. The most common endogenous opioid peptides produced in humans Рeptide Enkephalins Leu-enkephalin YGGFL Met-enkephalin YGGFM Metorphamide YGGFMRRV-NH2 Peptide E Peptide Sequence YGGFMRRVGRPEWWMDYQKRYGGFL Endorphins B-endorphin Y-endorphin a-endorphin YGGFMTSEKSQTPLVTLF KNAIIKNAYKKGE YGGFMTSEKSQTPLVTL YGGFMTSEKSQTPLVT Dynorphins Dynorphin A Dynorphin B Dynorphin1-8 YGGFLRRQ a-neoendorphin YGGFLRKYPK B-neoendorphin YGGFLRKYP YGGFLRRIRPKLKWDNQ YGGFLRRQFKWT 1. Endogenous opioids are peptides that are naturally produced in our bodies at low amounts and at specific times (see Table 1). These peptides bind to specific protein receptors in our nervous system that mediate pain signaling and reward. The chemical structure of an endogenous opioid peptide is shown below. но CHз S нн N. H2N HO н нн a) Determine the sequence of the peptide structure (in one-letter code): b) Based on the sequence and Table 1, what is the name of this peptide? c) How many of the alpha-carbons in the sequence are chiral (encircle one)? 1 2 3 4 5 6 d) How many peptide bonds are in the structure (encircle one)? 12 3 4 5 6 e) Identify all the peptide bonds by crossing out (place an X) at each peptide bond. f) How many ionizable functional groups are in the peptide (encircle one)? 1 2 3 4 5 6 g) Which amino acid in this peptide has a side chain that can form hydrogen bonds with water? Is this side-chain an H-bond donor, acceptor, or both? I ZI IZ о ZI I

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Table 1. The most common endogenous opioid peptides produced in humans Рeptide Enkephalins Leu-enkephalin YGGFL Met-enkephalin YGGFM Metorphamide YGGFMRRV-NH2 Peptide E Peptide Sequence YGGFMRRVGRPEWWMDYQKRYGGFL Endorphins B-endorphin Y-endorphin a-endorphin YGGFMTSEKSQTPLVTLF KNAIIKNAYKKGE YGGFMTSEKSQTPLVTL YGGFMTSEKSQTPLVT Dynorphins Dynorphin A Dynorphin B Dynorphin1-8 YGGFLRRQ a-neoendorphin YGGFLRKYPK B-neoendorphin YGGFLRKYP YGGFLRRIRPKLKWDNQ YGGFLRRQFKWT
Transcribed Image Text:Table 1. The most common endogenous opioid peptides produced in humans Рeptide Enkephalins Leu-enkephalin YGGFL Met-enkephalin YGGFM Metorphamide YGGFMRRV-NH2 Peptide E Peptide Sequence YGGFMRRVGRPEWWMDYQKRYGGFL Endorphins B-endorphin Y-endorphin a-endorphin YGGFMTSEKSQTPLVTLF KNAIIKNAYKKGE YGGFMTSEKSQTPLVTL YGGFMTSEKSQTPLVT Dynorphins Dynorphin A Dynorphin B Dynorphin1-8 YGGFLRRQ a-neoendorphin YGGFLRKYPK B-neoendorphin YGGFLRKYP YGGFLRRIRPKLKWDNQ YGGFLRRQFKWT
1. Endogenous opioids are peptides that are naturally produced in our bodies at low amounts and at specific times (see Table 1). These peptides bind to specific protein receptors in our nervous system that mediate pain signaling and reward. The chemical structure of an endogenous opioid peptide is shown below. но CHз S нн N. H2N HO н нн a) Determine the sequence of the peptide structure (in one-letter code): b) Based on the sequence and Table 1, what is the name of this peptide? c) How many of the alpha-carbons in the sequence are chiral (encircle one)? 1 2 3 4 5 6 d) How many peptide bonds are in the structure (encircle one)? 12 3 4 5 6 e) Identify all the peptide bonds by crossing out (place an X) at each peptide bond. f) How many ionizable functional groups are in the peptide (encircle one)? 1 2 3 4 5 6 g) Which amino acid in this peptide has a side chain that can form hydrogen bonds with water? Is this side-chain an H-bond donor, acceptor, or both? I ZI IZ о ZI I
Transcribed Image Text:1. Endogenous opioids are peptides that are naturally produced in our bodies at low amounts and at specific times (see Table 1). These peptides bind to specific protein receptors in our nervous system that mediate pain signaling and reward. The chemical structure of an endogenous opioid peptide is shown below. но CHз S нн N. H2N HO н нн a) Determine the sequence of the peptide structure (in one-letter code): b) Based on the sequence and Table 1, what is the name of this peptide? c) How many of the alpha-carbons in the sequence are chiral (encircle one)? 1 2 3 4 5 6 d) How many peptide bonds are in the structure (encircle one)? 12 3 4 5 6 e) Identify all the peptide bonds by crossing out (place an X) at each peptide bond. f) How many ionizable functional groups are in the peptide (encircle one)? 1 2 3 4 5 6 g) Which amino acid in this peptide has a side chain that can form hydrogen bonds with water? Is this side-chain an H-bond donor, acceptor, or both? I ZI IZ о ZI I
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