molecule0=FOFOOHOHOHtype of molecule(check all that apply)☐ fatty acidחחחחmonoglyceridediglyceridetriglyceridesaturatedunsaturated☐ monounsaturatedpolyunsaturatedw-3w-6☐ fatty acid☐ ☐ ☐ ☐monoglyceridediglyceridetriglyceridesaturatedunsaturatedmonounsaturatedpolyunsaturatedw-3☐ w-6fatty acidmonoglyceridediglyceridetriglyceridesaturated☐ unsaturated☐ monounsaturated☐ ☐ ☐polyunsaturatedw-3☐ w-6✗

The block diagram shows several rectangular blocks labeled with logic gates (OR, AND, NOT) and their…

Answered: molecule 0= FO FO OH OH OH type of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

What molecule allowed our target protein to elute off our affinity column? O a. lysozyme O b. BSA O c. imidazole O d. Laemmli O e. PMSF What information can isoelectric focusing provide about a protein? choose one or more: a. its pl b. its degree of purity c. its Km d. its molecular weight
Imagine you were able to incorporate real and artificial amino acids with the following side chains into proteins. Which of these would be most likely to be found on the outside surface of the hemoglobin protein in its folded form at ~pH 7.0? a) -CH2OH b) -phenol (phenyl with -OH) c) -phenyl d) -CH2CH3
A. What type of bond is ( the two mark wtih questions mark) B. What special amino acid side chain is involved in forming these bond C. Does this bond form unde reduction or oxidizing D. Is this bond seen more in cytoplsmic proteins or in extravellular protein
Which of the following statements are correct about protein folding (select all that appy)? A. Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation B. The mature two-chain form of insulin spontaneously folds into the native conformation C. A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates D. Proteins randomly sample each possible conformation before arriving final native state E. Proteins with disulfide bridges tend not follow a simple two-state folding mechanism.
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
Which of the following statements are correct about the molten globular state of protein folding (select all that appy)? A. May be short-lived or long-lived intermediate in protein folding B. Contains substantial levels of secondary structure C. Has loose packing of hydrophobic core D. Larger radius of gyration than dentaured state E. Is a more compact state than the native confomation
What are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.
Hi, please help with this question: What is the net charge on the amino acid cysteine at pH 8.0? (pKa values are α-carboxyl 2; α-amino 10; side chain 8) Thanks
1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation
Proteins treated with proteolytic enzymes hydrolyzed peptide bonds to yield a mixture of amino acids only. Is the statement TRUE OR FALSE?
Which of the following amino acids is most likely to be found on the outside of a soluble protein? Which is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globularform.)(a) Leucine (b) Glutamate(c) Phenylalanine (d) Glutamine
D raw the full structure of the following tetrapeptide . Label the N terminaland C terminal residues. Phe - Cys - Ser - Ile

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