1. The following protein crystal structure is the Human Serum Albumin complexed withoctadecanoic acid (PDB ID: 1E7I).According to the protein data bank, Human Serum Albumin is composed of 72% helical structure.Among the following options (a-c), select the possible Ramachandran plot for the above HumanSerum Albumin.(a)(b)(c)PhiPhiPhi 2. Fill in the blank: Identify the type of non-covalent/covalent interactions present in the followingprotein tertiary structure at physiological condition. Be specific about the type of interactions. 1H-O0-Hон онÇH,CH,CH,HCH,- NH;CH-OH0-CH,QQQ

The Ramachandran plot is a graph plot between phi (φ) and psi (ψ) the torsional angles of the…

2. Fill in the blank: Identify the type of non-covalent/covalent interactions present in the following protein tertiary structure at physiological condition. Be specific about the type of interactions. 1 H-O H. 0-H он он CH, CH3 CH NH CH.- OH 0–CH,

2. Fill in the blank: Identify the type of non-covalent/covalent interactions present in the following protein tertiary structure at physiological condition. Be specific about the type of interactions. 1 H-O H. 0-H он он CH, CH3 CH NH CH.- OH 0–CH,

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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5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
. Theoretical and experimental measurements show that in many cases, the contributions of ionic and hydrogen-bonding interactions to AH for protein folding are close to zero. Provide an explanation for this result.,
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1. (a) Arrange the following lipid molecules in the order of their relative melting points. Н.С — о-С-R Н.С — о-С-R H,C -0-ć- | НС —0—С-R НС —о-с-R' НС —о-с-R" H2C -0-Ċ-R H2C -0-C-R H2C -0-ċ-R" VI VII VIII (-olx). 0-ċ-R 180 —о-с-R 18-1 cisÃ9 -ċ-R") = 18:1transA9 (b) Give your reasons for your answer. (c) On heating lipid VI with aqueous NAOH, all the ester linkages were hydrolyzed. Draw the structure of each product of the hydrolysis. (e) Giving a reason for your answer, predict what would happen to the solubility of these products in water if, after the hydrolysis, excess acid was added to the medium to acidify it.
20. The dissociation constant of protein Z for ligand Y is: 10 micromolar. What fraction of the ligand is bound at ligand concentration = 5 micromolar?
Tt O 8. What are the driving forces that promotes tertiary -3D and quaternary -4D structure formation of proteins. Provide specific examples of the interactions that drive the formation of 3D and 4D structures?