In the figures of ferricrocin and enterobactin, circle the parts of the molecule that are b) responsible for metal binding (if you are using a separate sheet for your answers, simply draw the individual functional groups and indicate how many there are in each siderophore). What are these
Q: Based on the figure and the explanation in the textbook, what are the random chances that the…
A: Denaturation is the process by which proteins lose their native conformation. Ribonuclease A has 124…
Q: Determine the amino acid sequence of a polypeptide from the following data:Complete hydrolysis of…
A: A polypeptide is a long-chain polymer of amino acid, which is joined by a peptide bond. Since there…
Q: Which of these decapeptide is the most hydrophobic?
A: 1)Answer is option 1"3". It has total of 7 hydrophobic amino acids which are…
Q: Draw the following amino acids interactions: 1. H-bond - between -0H of Serine amino acid and C=0…
A: Between an electronegative atom with a lone pair of electrons and a hydrogen atom that is covalently…
Q: A HEPTAPEPTIDE that punctures the bacterial cell wall has just been recently isolated from the venom…
A: Acid hydrolysis of any protein/polypeptide is used to identify amino acids contained in the…
Q: Propose a method to determine the size and basic structure of chymotrypsin for the purpose of…
A: Any matter on the planet consists of atoms linked by interatomic bonds. The properties of the matter…
Q: (a) A solution containing these five proteins was adjusted to pH 7.0 and then applied to a…
A: Chromatography is a method of separation of specific compounds from the mixture of compounds. This…
Q: If mevalonate labeled with 14C in the carboxyl carbon were administered to rats, which carbons of…
A: The mevalonate pathway, or the isoprenoid pathway, also termed the 3-hydroxy-3-methylglutaryl-CoA…
Q: You are studying a catalytic protein which contains two ion clusters, one cluster contains 2 Cu+3…
A: Proteins are the biomolecules that are building blocks of the body. Proteins are made up of amino…
Q: Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in acqueous…
A: Amino acids are made up of two functional groups, an amino (-NH2) group, and a carboxyl (-COOH)…
Q: Which of the following peptides are consistent with the data below? 1. Amino acid analysis gave Met,…
A:
Q: Amino acid analysis of the peptide angiotensin II shows the presence of eight different amino acids…
A: Trypsin and chymotrypsin are proteolytic enzymes, which help to cleave the peptide bonds from…
Q: You are given two proteins with a pI of 4.5 and pI of 7.7. In an example of an anion-exchange…
A: Ion exchange chromatography is an isolation and purification technique used to separate biomolecules…
Q: Why is proline so common in the myoglobin and haemoglobin molecules at the points where the…
A: Proline is one of the twenty amino acids that is an imino acid. It is a non-essential amino acid…
Q: List the steps required for the cell to incorporate NH3 into aminoacids.
A: The amino acid plays a major role in the biological processes of all organisms and it acts as a…
Q: What generates the peak at 410 nm? a. The heme group of cytochrome c b. The heme group of bovine…
A: Absorbance is the optical density i.e. the quantity of light absorbed by the solution which is…
Q: Identify the parts of the heterotrimeric G-protein shown in the image. B
A: Introduction :- G proteins, also known as guanine nucleotide-binding proteins, are a group of…
Q: if i have protein with 110kda and its cysteine joining with disulfide bond . and one cysteine acids…
A: A chemical bond is a force of attraction between atoms or ions. Bonds form when atoms share or…
Q: A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare…
A: DNA sequencing is a biochemical method for determining the order of the nucleotide bases, adenine,…
Q: NH он NH2 LOH OH O NH, NH но HN OH HN NH2 NH он ÔH HN. OH NH HN NH2
A: Oligopeptides are also referred as peptide. Oligopeptide consists of 2 to 20 amino acids.
Q: What type of protein is included in milk? When milk sourness occurs, why does this protein…
A: Proteins are a linear chain of amino acid sequences attached together via peptide bonds. Proteins…
Q: What functions would you expect to be served by residues such as (a) phenylalanine at the protein…
A: Protein structures are formed by the three-dimensional arrangement of amino acids in a protein…
Q: What type of noncovalent interaction occurs between the glutamine and threonine side chains? Draw…
A: Non-covalent interactions are the weekly sharing of electrons between the atoms whereas it was an…
Q: A protein has an isoelectric point of 7 and you have two choices of resins. One is BioRex -70,…
A: Ion exchange chromatography is a type of column chromatography, for the separation and purification…
Q: You have a solution with an unknown amino acid. After running a few experiments, you discover the R…
A: Amino acids containing nitrogen in its R-group are- Glutamine, Asparagine, Lysine, Arginine and…
Q: The amino acid residue sequence of the hemoglobin beta subunit polypeptide would represent what type…
A: Hemoglobin, the protein present in the red blood cells is responsible for the transport of gases…
Q: Consider the image of the attached protein. Now imagine you have a proteolytic enzyme that cleaves…
A: The mentioned proteolytic enzyme cleaves the peptide-bonds on the C-terminal sides of basic amino…
Q: A structural difference between uracil and cystosine is: A. At C-4 cytosine has an amino group,…
A: Nucleic acids are one of the most important organic compounds. A combination of a sugar molecule,…
Q: In what type of intra and intermolecular interactions does a valine within a protein backbone…
A: Hemoglobin A is composed of two α and two β-globin chains along with the heme molecule which…
Q: A HEPTAPEPTIDE that punctures the bacterial cell wall has just been recently isolated from the venom…
A: Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…
Q: An amino acid mixture consisting of lysine,leucine, and glutamic acid is to be separated by…
A: In reverse-phase HPLC with a non polar stationary phase and a polar solvent as the mobile phase at…
Q: What is the molecular weight of the Botulinum neurotoxin, a protein that contains 1350 amino acids?…
A: Given Values: Number of residues present in botulinum toxin = 1350
Q: For the 3 molecules in the image, explain if the nitrogen can act as a hydrogen bond acceptor or not…
A: There are different types of bonds formed between atoms to form a molecule. The different types of…
Q: A mixture of Asparagine (pl 5.41) , Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74)…
A: Cation exchange chromatography separates the molecules based on their net negative charge. Cation…
Q: Our body is compost of about 70% water which means that majority of the chemical processes happens…
A: The amino acids are classified based on the polarity as, Polar amino acids (hydrophilic)- These are…
Q: What is the structural basis for enzyme specificity?
A: Enzymes are essentially proteins that act as a catalyst for biological reactions. They act by…
Q: Using the data in the table below, calculate the average molar mass of an amino acid residue in each…
A: Proteins are unbranched polymers constructed from 20 standard α-amino acids. They have four levels…
Q: Why is it not recommended to use reconstituted or evaporated milk? Why is full cream milk suggested…
A: The United States Public Health Service defines Recombined milk or Reconstituted milk as an…
Q: The tertiary structures of the alpha and beta subunits of Hb are examples of which type of…
A: Hemoglobin is defined as the protein molecule present in RBCs carrying oxygen from the lungs to the…
Q: Consider a hexapeptide of the sequence thr asn glu trp lys gln. A researcher decided that this…
A: The hexapeptide contains 6 amino acids - thr, asn, glu, trp, lys, gln.
Q: Why is Indole more likely to travel through the cell membrane than tryptophan? The image here shows…
A: Any molecule can transfer across a protein free lipid bilayer over a variable period of time due to…
Q: Describe in detail the composition and structure of peptidoglycan. Why does peptidoglycan contain…
A: Peptidoglycan is found in the bacterial cell walls. Peptidoglycan helps in the immune response. It…
Q: Most protein dissolve in neutral salt solution, is that true? Provide reasoning
A: When the salts are added to increase the solubility of protein and dissolve protein is known as…
Q: Which of the following is NOT a unit of concentration? All of these options are units of…
A: The specific activity is the activity of the enzyme present per milligram of the total enzyme.
Q: Tryptophan is not classified as a basic amino acid even though it has aheterocycle containing a…
A: Introduction: Tryptophan is categorized as an essential amino acid that cannot be produced by the…
Q: What is a putative substrate? Is it the ligand that binds to the protein? And how am I supposed to…
A: The term putative in biology is commonly applied to explain the concept that is generally accepted…
Q: Can you please describe the specific components that each of these structures are comprised of (…
A: Proteins are the biomolecules which are made up of amino acids. Amino acids are joined together with…
Q: Draw the structure of a D-glucose molecule linked to threonine via a β-glycosidic linkage.
A: The amino derivative of glucose is known as an N-aceltyglucoseamine. where it forms a secondary…
![In the figures of ferricrocin and enterobactin, circle the parts of the molecule that are
b)
responsible for metal binding (if you are using a separate sheet for your answers, simply draw the
individual functional
and indicate how many there are in each siderophore). What are these
groups
called?
functional
groups
c)
What are the coordination geometries and the overall charges on the metal complexes of
ferricrocin and enterobactin?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Faf13ae8a-67d3-42d3-9379-32c723e10b0f%2F2bbe357e-01e8-4828-80a8-b58bc733b400%2F2njd2e_processed.png&w=3840&q=75)
![3) Consider the structures of the siderophores ferricrocin (left) and enterobactin (right) below.
OH
HO,
ÓH
NH
Он
HO
OH
HN.
но.
HO
но](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Faf13ae8a-67d3-42d3-9379-32c723e10b0f%2F2bbe357e-01e8-4828-80a8-b58bc733b400%2F4k00l8bj_processed.png&w=3840&q=75)
![](/static/compass_v2/shared-icons/check-mark.png)
Step by step
Solved in 2 steps with 2 images
![Blurred answer](/static/compass_v2/solution-images/blurred-answer.jpg)
- 3c.) Now, diagram below the internal structure of each villus Make sure to carefully depict the microvilli brush border and the system of vessels within each villus. Identify in your drawing the path taken by water-soluble versus fat-soluble nutrients once absorbed in the intestinal villi. (Describe what is the purpose Enterotube II/ Enteropluri system? (In detail)3. The gall stones were found in the patient by the upper abdominal ultrasound investigation. Explain the causes of the gall stones formation. For that: a) describe the composition of bile and the functions of the main bile compounds; b) draw the scheme of the bile salts synthesis and conjugation; c) describe the fate of secondary bile salts and their function in cholesterol metabolism; d) explain the way of the gall bladder stones formation.
- ESOPHAGUS 1. The esophagus takes food from the to the 2. a) At the junction of the esophagus and the stomach is a circular smooth muscle called the b) Contraction of this sphincter prevents the backup of into the3. Clinicians work on the case of a patient with chronic pancreatitis. This disease leads to insufficient secretion of the pancreatic juice into the small intestine. What changes in the dietary lipid processing that discase will cause? For the answer: a) draw the reactions of TAG digestion and the conditions they require; b) list all possible consequences of lipid indigestion; c) list the essential lipid compounds that would have a faulty absorption due to this discase; d) name the other detrimental causes of lipid indigestion and malabsorption.1.A patient with chronic pancreatitis and hence decreased secretory function of pancreas was prescribed an enzymatic drug «Enzystal» before each meal. Explain this prescription. For that: a)Name pansreatic enzymes, participating in digestion of carbohydrates, lipids and proteins. What is their pH optimum and how is it reached in duodenum? b) Draw the scheme representing the cascade of activation of pancreatic proteolytic enzymes. Indicate the mechanism ofactivation and its reversability c)Why are proteolytic enzymes secreted by pancreas in inactive form? d)What recommendations on diet can be given to this patient?
- Define the following terms: a. enterocyte b. lipoprotein lipase c. ApoB-48 d. ApoE e. ApoC-II1. List the following organs in sequence from mouth to anus: caecum, colon, duodenum, esophagus, ileum, jejunum, laryngopharynx, oral cavity, oropharynx, rectum, stomach -> Mouth > -> -> -> -> -> → anus -> ->34) Bile….which one of the following is clearly incorrect? a. initiates emulsification of lipids b. contains bicarbonate c. is produced in the liver and pancreas d. is stored in the gall bladder e. despite acting as a detergent, it’s primary component is water
- 4. A patient with food indigestion has been screened and diagnosed with steatorrhea (the excretion of abnormal quantities of fat with the feces owing to reduced absorption of fat by the intestine). What are the causes and consequences of the steatorrhea? For the answer: a) draw the scheme of TAG digestion; b) explain the role of the pancreas in dietary lipid digestion; c) make a scheme of dietary TAG assimilation up to the step of chylomicron formation; d) list the dietary recommendation for that particular patient.12. Use the following photo and identify these organs: Diaphragm Duodenum Gallbladder Kidney Large intestine Liver Pancreas Rectum Renal artery Small intestine Spleen Stomach Ureters (Urinary) bladderGut commensal bacteria are beneficial to animal nutrition including humans. For non-fermenting animals such as humans, select the answer that describes the greatest benefit of gut microflora on nutritional physiology. Select one: a. Absorption of carbohydrates b. Removal of water c. Production of some types of essential vitamins such as biotin and vitamin K d. Generation of gases necessary for proper elimination