Protein folding with PDI and Peptidyl-prolyl isomerase
Q: The defining characteristics of amino acids and how the 20 amino acids involved in protein structure…
A: Each of the 20 most common amino acids has its specific chemical characteristics and its unique role…
Q: 57. An increase in the ratio of saturated to unsaturated fatty acid chains in a membrane…
A: Lipids are macromolecules made up of carbon, hydrogen, and oxygen just like carbohydrates but in…
Q: How many alpha helices comprise this structure (2JHO-myoglobin)? Number the helices with helix 1 at…
A: The α-helix is a polypeptide backbone & a structural unit that can be distinguished to shifting…
Q: how cohesin acts as the glue
A: Cohesin is a complex of multiple protein units that is responsible for holding together the sister…
Q: Red blood cells are normally circular in shape. Sickle cell anemia is a disorder that affects the…
A: sickle cell anemia is a genetic disorder caused by alternation in genetic sequence .
Q: Comparision between neutral amino acid (tyrosine) and cyclic alcohol
A: Amino acids are monomers of protein they are linked with each other by forming peptide…
Q: Upload a drawing of Gly-Met-Asn-Glu-His Label the alpha carbons Label the R groups as…
A: Alpha carbon: It is the carbon connecting the amino group and carboxylic group in amino acid. Acidic…
Q: ophobio, amPNo acius on the inside of the three-dimensional shape 3. Which sentences are'true: a. in…
A: The amino acids and the derivatives of the amino acids possess diverse functions in the body. The…
Q: how the structure of arachidonic is suited for the synthesis of PGG2.
A: Prostaglandins are C20 fatty acids that have been changed and produced in animal tissues. They have…
Q: how to draw tripeptide alanyl-glutamyl-glycine (AEG)
A: Amino acids are biomolecules made up of two functional groups, these are an amino group (-NH2) and a…
Q: The number of distinct protein folds in limited. Why might this be so?
A: Protein folding is the physical process by which a polypeptide folds into its characteristic…
Q: why the notation Ala-Gly-Val-Ala and Ala-Val-Gly-Ala represent two different molecules rather than…
A: The primary structure of protein is a sequence of amino acids. The secondary structure includes…
Q: 6. heparin contains more than one type of sugar residues
A: Heparin is a naturally occurring glycosaminoglycan. It is an anticoagulant that occurs in blood,…
Q: sequence of amino acids.
A: The central dogma of molecular biology is the concept which explains the flow of genetic…
Q: Regular and irregular secondary protein structures
A:
Q: Color Reactions of Intact Protein: 1ml of water and 0.5 g of casein 1ml of water and 0.5 g of bean…
A: All proteins do not contain the same amino acids hence they do not respond to all colour reactions…
Q: Sequence of Carminic acid
A: Carminic acid is a type of red dye that is extracted from various insect taxa like- Kermes vermilio,…
Q: Definition of the concept of "amino acid". The main parts of the amino acid molecules. Alpha, beta,…
A: Amino acids are building blocks of proteins, which polymerize to form different kinds of proteins.…
Q: Amyloid fibers, which are insoluble and are the source of mad cow disease, alzheimer disease, and…
A: A protein is considered to be a biological macromolecule made up of one or more polypeptide…
Q: A common calcium-binding motif called the __________ contains twoshort helices connected by a loop
A: Calcium-binding proteins are responsible for binding to calcium. Various types of calcium-binding…
Q: Peptides Drawing and Naming Peptides 1.) Glu-Ser-Ala 2.) Gly-Tyr-Leu-Val
A: The peptides are short chains made of less than 20 amino acids. The proteins are made of more than…
Q: A secondary structure of proteins in which the peptide has regular coils and every N-H group…
A: Local folded structures that arise within a polypeptide as a result of interactions between backbone…
Q: pentose phosphate
A: 5. The pentose phosphate pathway is a kind of metabolic pathway that is alternate to the glycolysis…
Q: DNA True or false A long chain polymer in which the internucleotide linkages are of the diester…
A: DNA is double-stranded in which two strands run in opposite directions. The secondary structure of…
Q: why glutamate is the most soluble in water at pH7
A: Amino aids are the monomers of polypeptide chains that make up proteins. There are a total of 20…
Q: No plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different…
A: Note : Hi ! Thank you for the question. We are authorized to answer one question at a time. Since…
Q: Chemical properties of fatty acids. Determination of the titer of higher fatty acids in solution.…
A: Fatty acids play an important role of fat in our bodies and food. Fats are broken down into fatty…
Q: Unique features and function of: Cysteine Lysine Proline Glutamic acid or Glutamine Tyrosine…
A: An amino acid is an organic compounds that contain alpha amino and alpha carboxylate functional…
Q: How multiple domains in a single protein increases the versatility of each molecule ?
A: A protein domain is a region in a protein molecule or polypeptide chain of protein which is…
Q: Contribution of the features of the alpha-helix to the stability of the protein.
A: Protein play wide variety of essential function in our body. They provide strength and structural…
Q: why all amino acids except glycine have L and D forms and specify the type of isomerization…
A: Amino acids are the monomeric units of proteins. The general structure of an amino acid has a…
Q: How many different polypeptides of 50 amino acids in length can be made from the 20 common amino…
A: Introduction: Amino acids are biomolecules that are comprised of two functional groups that are an…
Q: structure of phosphatidylinositol that contains oleic acid and arachidonic acid
A: Fatty acids are also lipids with carboxylic acid group attached to long hydrocarbon chain. If there…
Q: Physiological Significance of all amino acids
A: Solution Aspartate - in urea cycle, aspartate and ammonia donate amino groups leading to formation…
Q: Difference between polypeptide and protein
A: A peptide is two or more amino acids joined together by peptide bonds; a polypeptide is a chain of…
Q: Common structural feature of Chitin and Amylopectin and Differences of chitin and amylopectin
A: The polysaccharides molecules are monosaccharides that are connected by glycosidic linkages.
Q: HN H H H H H Se он
A: Peptides or proteins are composed of twenty standard amino acids attached together via peptide…
Q: Unique features and function of all 20 major amino acids
A: Amino acids form a larger component of the body in the form of proteins. They are generally divided…
Q: Proteinogenic amino acids, their quantity, what is the reason. Distinctive features of proteinogenic…
A: Amino acids are the building blocks of proteins, which play a vital role in synthesizing proteins…
Q: Structural formula of a fat molecule (triglyceride) made of myristic acid, oleic acid, palmitic…
A: Triglycerides are triesters of glycerol and long-chain carboxylic acids called fatty acids. In…
Q: difference between partially hydrolyzed protein and completely hydrolyzed protein
A: Proteins are biomolecules made up of long chains of amino acids linked by a peptide bond which serve…
Q: .solubility of vitamins
A:
Q: Chiral carbon atom not present in: * Erythrose Dihydroxyacetone
A: Erythrose is a four carbon aldose sugar. Erythrulose is a four carbon ketose sugar. Glyceraldehyde…
Q: Biological significance of protein
A: Proteins are biopolymers made of monomeric units called amino acids. The amino acids are of…
Protein folding with PDI and Peptidyl-prolyl isomerase
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- 11:14 structure. They provide the matrix or ground substance of extracellular tissue spaces in which collagen and elastin fibers are embedded. Hyaluronic acid, chondroitin 4-sulfate, heparin, are among the important glycosaminoglycans. 10. Glycoproteins are a group of biochemically important compounds with a variable composition of carbohydrate (1-90%), covalently bound to protein. Several enzymes, hormones, structural proteins and cellular receptors are in fact glycoproteins. Chapter 2: CARBOHYDRATES SELF-ASSESSMENT EXERCISES I. Essay questions 1. Define and classify carbohydrates with suitable examples. Add a note on the functions of carbohydrates. 2. Describe the structure and functions of mucopolysaccharides. 3. Give an account of the structural configuration of monosaccharides, with special reference to glucose. 4. Discuss the structure and functions of 3 biochemically important disaccharides. 5. Define polysaccharides and describe the structure of 3 homopolysaccharides. III. Fill…Upload a drawing of Gly-Met-Asn-Glu-His Label the alpha carbons Label the R groups as hydrophobic or hydrophilic Label the acidic and basic R-groups Label the peptide bonds Label the N terminus and the C terminusThe number of distinct protein folds in limited. Why might this be so?
- Part C Calculate to three decimal places the charge on a-melanotropin at pH value of 5. Express your answer using three decimal places. VE ΑΣΦ Submit Request Answer Part D Calculate to three decimal places the charge on a-melanotropin at pH value of 1. Express your answer using three decimal places. VE ΑΣΦ Submit ? Request Answer ?structure of phosphatidylinositol that contains oleic acid and arachidonic acidClassification of amino acids by radicals, on what it is based. Name and draw radicals of each type of proteinogenic amino acids.
- cip sequence rule in ephedrineCommon structural feature of Chitin and Amylopectin and Differences of chitin and amylopectinHydropathy & Amphipathicity 2 -1 -2- 110 210 310 410 510 Residue Number C. Draw the topology of this membrane protein in the bilayer and indicate the range of residues forming transmembrane a-helices.
- Protein Structure and Function A common strategy in the regulation of protein function is to alter its structure. Describe two specific strategies used by the cell to alter a protein’s structure, thereby altering its function.One round of Edman degradation of the peptide: H2N- Gly-Arg-Lys- Phe-Asp- COOH which of the following structures would result when add cyanogen bromide ? A) H2N-Gly-Arg-COOH + H2N–Lys-Phe- Asp-COOH B) H2N-Arg-Lys-Phe-Asp-C0OH+ Gly C) H2N- Gly-Arg-Lys-Phe-Asp- COOH D) H2N-Gly-Arg-Lys-Phe-COOH + Asp E) H2N-Gly-Arg-Lys-COOH + H2N-Phe-Asp-COOHActivity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartate