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below). The red arrow indicates the amino acid lysin (K) that binds to the oxygen of the retinol (indicated by the blue arrow). The purple arrow indicates the retinal bound to the rhodopsin. In healthy individuals, retinal is abundant and can binds to the rhodopsin, making it functional (light-sensitive). H3C CH3 CH3 cytoplasmic side 0000 000 CH3 Retinal extracellular side C-I OO CO LOOD CO00 000 0000 000 CH3 COO 000 0000 GUIA 000 000 000 0000 0030 0000 000 C-II 000 000 CO @o Rhodopsin (primary structure) FOO OCK NOWE OV00 OPO 000 0600 DOOO 0000 COO COO 0000 0000000 Gooo 9000 E-II COOH-terminal C-III OO 200 000 DOO 000 000 E-III Čoooo NH₂-terminal Rhodopsin + retinal (tertiary structure) 6. This lysine (K) is in a transmembrane domain of rhodopsin and can bind to retinal. Based on the chemical property of lysine, which of the following can you conclude? A. Lysine is a hydrophobic amino acid that binds to water molecules, hydrophobic tails of phospholipids and to retinal B. Lysine is a negatively charged amino acid that has a high affinity for the hydrophobic tails of phospholipids C. Lysine is a positively charged amino acid that has a high affinity for the hydrophobic tails of phospholipids D. Lysine is a hydrophilic amino acid oriented towards the hydrophobic tails of the phospholipids and can bind to them E. Lysine is a positively charged amino acid that does not interact with hydrophobic tails of the phospholipids but instead is located inside the rhodopsin (in its tertiary structure) and binds to the electronegative oxygen of retinal

below). The red arrow indicates the amino acid lysin (K) that binds to the oxygen of the retinol (indicated by the blue arrow). The purple arrow indicates the retinal bound to the rhodopsin. In healthy individuals, retinal is abundant and can binds to the rhodopsin, making it functional (light-sensitive). H3C CH3 CH3 cytoplasmic side 0000 000 CH3 Retinal extracellular side C-I OO CO LOOD CO00 000 0000 000 CH3 COO 000 0000 GUIA 000 000 000 0000 0030 0000 000 C-II 000 000 CO @o Rhodopsin (primary structure) FOO OCK NOWE OV00 OPO 000 0600 DOOO 0000 COO COO 0000 0000000 Gooo 9000 E-II COOH-terminal C-III OO 200 000 DOO 000 000 E-III Čoooo NH₂-terminal Rhodopsin + retinal (tertiary structure) 6. This lysine (K) is in a transmembrane domain of rhodopsin and can bind to retinal. Based on the chemical property of lysine, which of the following can you conclude? A. Lysine is a hydrophobic amino acid that binds to water molecules, hydrophobic tails of phospholipids and to retinal B. Lysine is a negatively charged amino acid that has a high affinity for the hydrophobic tails of phospholipids C. Lysine is a positively charged amino acid that has a high affinity for the hydrophobic tails of phospholipids D. Lysine is a hydrophilic amino acid oriented towards the hydrophobic tails of the phospholipids and can bind to them E. Lysine is a positively charged amino acid that does not interact with hydrophobic tails of the phospholipids but instead is located inside the rhodopsin (in its tertiary structure) and binds to the electronegative oxygen of retinal

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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The amino acid sequence (primary structure) and 3D shape (tertiary structure) of the rhodopsin has been determined and the various protein domains have also been identified with precision (see figures below). The red arrow indicates the amino acid lysin (K) that binds to the oxygen of the retinol (indicated by the blue arrow). The purple arrow indicates the retinal bound to the rhodopsin. In healthy individuals, retinal is abundant and can binds to the rhodopsin, making it functional (light-sensitive). H3C CH3 CH3 CH3 cytoplasmic side Retinal C-I extracellular side 0000 MOO OOO 400 DERY 000 PONE ALMO VOO LGF LLOD VUEL CH3 HOO AD SLV GO04 FAV OCK 000 LOO GOF YO DOAA TOTO ⓇAD MOWE OV00 OPL ALA LEGE DOOD VOOO COP DES 000 600 GCO OV FOOD Rhodopsin (primary structure) C-II E-II COOH-terminal C-III RIVE OOM DOWO LWCO 40 DOVO FOX ON DO 000 D04 boooooo 000 000 100,00 ****** E-III NH₂-terminal Rhodopsin + retinal (tertiary structure) 6. This lysine (K) is in a transmembrane domain of rhodopsin and can bind to retinal. Based on the chemical property of lysine, which of the following can you conclude? A. Lysine is a hydrophobic amino acid that binds to water molecules, hydrophobic tails of phospholipids and to retinal B. Lysine is a negatively charged amino acid that has a high affinity for the hydrophobic tails of phospholipids C. Lysine is a positively charged amino acid that has a high affinity for the hydrophobic tails of phospholipids D. Lysine is a hydrophilic amino acid oriented towards the hydrophobic tails of the phospholipids and can bind to them E. Lysine is a positively charged amino acid that does not interact with hydrophobic tails of the phospholipids but instead is located inside the rhodopsin (in its tertiary structure) and binds to the electronegative oxygen of retinal
Transcribed Image Text:The amino acid sequence (primary structure) and 3D shape (tertiary structure) of the rhodopsin has been determined and the various protein domains have also been identified with precision (see figures below). The red arrow indicates the amino acid lysin (K) that binds to the oxygen of the retinol (indicated by the blue arrow). The purple arrow indicates the retinal bound to the rhodopsin. In healthy individuals, retinal is abundant and can binds to the rhodopsin, making it functional (light-sensitive). H3C CH3 CH3 CH3 cytoplasmic side Retinal C-I extracellular side 0000 MOO OOO 400 DERY 000 PONE ALMO VOO LGF LLOD VUEL CH3 HOO AD SLV GO04 FAV OCK 000 LOO GOF YO DOAA TOTO ⓇAD MOWE OV00 OPL ALA LEGE DOOD VOOO COP DES 000 600 GCO OV FOOD Rhodopsin (primary structure) C-II E-II COOH-terminal C-III RIVE OOM DOWO LWCO 40 DOVO FOX ON DO 000 D04 boooooo 000 000 100,00 ****** E-III NH₂-terminal Rhodopsin + retinal (tertiary structure) 6. This lysine (K) is in a transmembrane domain of rhodopsin and can bind to retinal. Based on the chemical property of lysine, which of the following can you conclude? A. Lysine is a hydrophobic amino acid that binds to water molecules, hydrophobic tails of phospholipids and to retinal B. Lysine is a negatively charged amino acid that has a high affinity for the hydrophobic tails of phospholipids C. Lysine is a positively charged amino acid that has a high affinity for the hydrophobic tails of phospholipids D. Lysine is a hydrophilic amino acid oriented towards the hydrophobic tails of the phospholipids and can bind to them E. Lysine is a positively charged amino acid that does not interact with hydrophobic tails of the phospholipids but instead is located inside the rhodopsin (in its tertiary structure) and binds to the electronegative oxygen of retinal
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