What is the purpose of having a sex hormone binding protein within the blood stream? What is the purpose of having a specific receptor for estrogen within the cell? The estrogen receptor binding domain has many known mutations that effect estrogen binding and result in breast cancer. One particular mutation found at aspartic acid is changed to glycine in cancer patients. Draw a potential interaction with the side chain of this aspartic acid with estrogen (name and label it) and how a mutation to glycine could affect this ability to efficiently bind to estrogen. 6.

What is the purpose of having a sex hormone binding protein within the blood stream? What is the purpose of having a specific receptor for estrogen within the cell? The estrogen receptor binding domain has many known mutations that effect estrogen binding and result in breast cancer. One particular mutation found at aspartic acid is changed to glycine in cancer patients. Draw a potential interaction with the side chain of this aspartic acid with estrogen (name and label it) and how a mutation to glycine could affect this ability to efficiently bind to estrogen. 6.

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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A mutant form of polypeptide hormone has the following amino acid composition: Asp, Arg, lle, Met, Phe, Pro, Tyr. Val The following observations are made: Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro, and a hexapeptide containing all the others. Chymotrypsin cleaves the hormone into two tetrapeptides with the following composition: (Asp, Arg, Tyr, Val) and (lle, Met Phe, Pro) The dipeptide of composition (Pro, Phe) cannot be cleaved by either chymotrypsin or carboxypeptidase. What is the amino acid sequence of this polypeptide?
A mutant form of polypeptide hormone has the following amino acid composition: Asp, Arg, lle, Met, Phe, Pro, Tyr, Val The following observations are made: Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro, and a hexapeptide containing all the others. Chymotrypsin cleaves the hormone into two tetrapeptides with the following composition: (Asp, Arg, Tyr, Val) and (lle, Met Phe, Pro) What is the amino acid sequence of this polypeptide?
One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below: 1) Provide a brief explanation as to why ligand binding to proteins must be a reversible process. 2) Calculate the dissociation constant (Kd) for the hormone binding to each of the three proteins. 3) Which of the proteins demonstrate the tightest/strongest binding of the hormone? Which demonstrates the least tight binding of the hormone? What is the basis for your answer?
The melatonin receptor exists in different isoforms: MT1, encoded by MT-1 gene and MT2, encoded by MT-2 gene. The following is the sequence corresponding to 90-140 base pairs (bp) of MT-1 and MT-2 genes. Which of the following statements are true for these DNA sequences. Select all that apply. 90 140 MT-1: 5'------GATATGCCCCCCCCGGCGCGCGATATGCCCCCCCCGGCGCGCGTGCGTGA -3' 3'------CTATACGGGGGGGGCCGCGCGCTATACGGGGGGGGCCGCGCGCACGCACT- -5' 90 140 ---GATATGATATATATATATATAGATATGAAAAATTTTTATATAGTGCGTGA- MT-2: 5' ---3' 3'-----CTATACTATATATATATATATCTATACTTTTTAAAAAATTATCACGCACT-- ----5' MT-2 will denature at a higher temperature than MT-1 1 MT-2 will denature at a lower temperature than MT-1 MT-1 will denature at a higher temperature than MT-2 MT-1 will denature at a lower temperature than MT-2
Trelstar® is an injectable formulation of polylactide-co-glycolide (PLGA) microspheresencapsulating triptorelin palmoate (Mw 13115 Da), a synthetic decapeptide agonist analog ofgonadotropin releasing hormone (GnRH). The medicine is used in treatment of patients withprostate cancer. The pharmacokinetics of triptorelin palmoate as free drug follows a 3 compartmentmodel with drug half-lives estimated to be 6 minutes, 45 minutes, and 3 hours, respectively. Threedifferent dosing intervals of Trelstar® are available in clinic: 1 month (3.75 mg), 3 month (11.25mg) and 6 month (containing 22.5 mg of drug).Discuss how encapsulation into PLGA microspheres improves patient therapy with triptorelinpalmoate, and how three dosing intervals available in clinic may have been achieved bymodifications in the formulation
At puberty, the adolescent human body undergoes changes in both structure and function of several organ systems, primarily under the influence of estrogen and testosterone steroid hormones. Which of the following best explains how two molecules can trigger many different types of systemic changes that occur during adolescence? A Estrogen and testosterone are both produced in very large concentrations by nearly ev- ery cell in the body. B с D Estrogen and testosterone bind to specific receptors inside many types of cells, each with different signal transduction pathways. Estrogen and testosterone bind to different membrane-bound receptors on different cells, initiating different transduction pathways. Estrogen and testosterone are able to cross the membrane of some cells but not others.
A study is conducted to assess the molecular mechanisms of hormone X. A radioactively labeled form of this hormone is incubated with human cells in tissue culture for 30 minutes, and then incubated briefly with a cross-linking agent. The plasma membrane, cytosolic, and nuclear fractions are isolated from the cell lysate, and the subcellular proteins are separated from these fractions by gel electrophoresis. The only protein bound to the labeled hormone is identified in the new clear fraction. Hormone X is most likely which of the following? Epinephrine Glucagon Growth hormone Insulin Thyroxine
Show where trypsin and chymotrypsin would cleave the following peptide. Tyr-Ile-Gln-Arg-Leu-Gly-Phe-Lys-Asn-Trp-Phe-Gly-Ala-Lys-Gly-Gln-GlnB. After treatment with peroxyformic acid, the peptide hormone vasopressin is partially hydrolyzed. The following fragments are recovered. Propose a primary structure for vasopressin.Phe-Gln-Asn Pro-Arg-Gly • NH2 Cys-Tyr-Phe Asn-Cys-Pro-Arg Tyr-Phe-Gln-AsnC. Consider the following peptide: Gly-Ile-Glu-Trp-Thr-Pro-Tyr-Gln-Phe-Arg-LysWhat amino acids and peptides are produced when the above peptide is treated with each of the following reagents?1. Carboxypeptidase2. Chymotrypsin3. Trypsin 4. DNFBD. From the analytical results, deduce the primary structure of a peptide isolated from the Atlantian orchid that contains 14 amino acids.Complete hydrolysis produces the following amino acids: Gly (3), Leu (3), Glu (2), Pro, Met, Lys (2), Thr, Phe. Treatment with carboxypeptidase releases glycine. Treatment with DNFB releases DNP- glycine. Treatment with a…
Hormone H regulates these effects via its receptors which are found at both the cell surface (csRH) and within the cell (içRH). The signalling pathways that become activated in the presence of hormone H are depicted and described below. hormone H. H H extracellular fluid inactive GTP inactive RAS Lyn cell-surface receptor for H (csR») icR GDP RAS-GTP hexose metabolism cell survival H icR G, phase (resting) Raf HK GSK-3P MEK M G2 icR - hexose kinase ERK promoter HRE CDK1 Cyclin A nucleus cyclin A Fos A promoter Created in BioRender.com bio Signalling via the cell surface receptor Hormone H mediates its cell cycle stimulatory and pro-survival effects by binding to and activating the cell surface hormone H receptor (csRH). The activated CSRH activates Lyn, which activates RAS and ultimately the Raf/MEK/ERK kinase cascade. Active ERK: o phosphorylates and inactivates GSK-3B. Inhibition of GSK-3ß promotes cell survival. inhibits p27, preventing it from inhibiting cell cycle progression.…
Ligand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below 1) Which of the proteins demonstrate the tightest/strongest binding of the hormone? Which demonstrates the least tight binding of the hormone? What is the basis for your answer?
Mutations were introduced into a type I receptor of steroid hormone X. Two classes of mutants were obtained. Class I mutants were severely defective in receptor-HSP (heat shock protein) interaction and class II mutants could not form receptor dimers. What effect the two classes of mutations will have on expression of genes controlled by hormone X?
Ligand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below: 1) Provide a brief explanation as to why ligand binding to proteins must be a reversible process. 2) Calculate the dissociation constant (Kd) for the hormone binding to each of the three proteins.