Why is alpha (a) the predominant anomeric form of mannose?A. The alpha-anomer is more unstable because of the presence of more axialsubstituentsB. The beta-anomer is more unstable because of the delta-2 effect of stericrepulsions between the lone pairs of the equatorial OH at C1 and the axial OHat C2C. The beta-anomer is more unstable because of the steric repulsions betweenthe lone pairs of the equatorial OH at C1 and C2D. Although the alpha-anomer has more axial OH, the instability factorscreated by one is cancelled by the other.E. The alpha-anomer creates a more open structure than the beta-anomer.

Mannose is a monosaccharide and it is also called a polyhydroxy aldehyde. It means mannose is an…

Answered: Why is alpha (a) the predominant…

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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Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.5; Pk2 = 10.8; PkR = 8.5 His: Pk1 = 1.6; Pk2 = 9.0; PkR = 7.0 Lys: Pk1 = 2.2; Pk2 = 8.5; PkR = 9.8 a.draw the protonic equilibria for the tripeptide. b.what is the IpH? c.What is the dominant structure at pH 3.0? d.What is the first buffering region of the tripeptide?
The melting curve for the polyribonucleotide poly(A) is shown below. (a) Explain why absorbance increases with increasing temperature. (b) Why does the shape of the curve differ from the one shown in Fig. ?
Draw the pyranose form of D-Glucose as a Haworth projection. Identify your projection as either the alpha or beta anomer. Which anomer of D-Glucose is more stable? Why?
Draw the (B1-->A1) linked dissacharide formed between the C3 epimer of B-D-glucose and the C2 epimer of a-D-galactose. Explain in 1-2 sentences why (or why not) a precipiate would be observed when mixing this dissacharide in an alkaline solution of copper.
A) Draw the "standard" base pairs (A:T and G:C) but instead of using the most common form of each base, use the uncommon tautomer form of each base (i.e. imino A, imino C, enol G, enol T). Clearly indicate hydrogen bonds (an arrow from donor to acceptor will suffice). Be sure to include the “R” representing the pentose. B) The G:U "wobble" base pair can be formed between the most common tautomer forms of G & U. Another base pair with the same geometry/pairing/orientation can be formed between G & T. Can you create a "wobble" base pair between the uncommon enol tautomer forms of G & T? Like the "wobble" G:U base pair in the Lecture 1 slides, this enol-based "wobble" G:T base pair must have at least two hydrogen bonds. If possible, draw such a base pair, and note any important differences from the non-enol G:U/T wobble. If it is not possible to draw such a base pair, explain why.
Draw the following sugars using Haworth projections:a. b-d-galactopyranose b. a-d-tagatopyranose c. a-l-glucopyranose
Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 = 9.17; PkR = 6.0 Lys: Pk1 = 2.18; Pk2 = 8.95; PkR = 10.53 draw the protonic equilibria for the tripeptide what is the IpH? What is the dominant structure at pH 2.0? What is the first buffering region of the tripeptide?
Raffinose is a trisaccharide and a minor constituent in sugar beets. (a) Is raffinose a reducing sugar?Explain. (b) What are the monosaccharides that compose raffinose ? (c) β - Galactosidase is an enzyme that will remove galactose residues from an oligosaccharide. What are the products of β - galactosidase treatment of raffinose ?
Draw a Haworth projection and Fischer projection for a methyl a-D-mannopyranoside (methyl a-D-mannoside). Label the anomeric carbon and the glycosidic bond.
Carboxypeptidase, which sequentially removes carboxyl-terminal amino acid residues from its peptide substrates, is a single polypeptide of 307 amino acids. The two essential catalytic groups in the active site arefurnished by Arg 145 and Glu 270 .(a) If the carboxypeptidase chain were a perfect α helix, how far apart (in Å) would Arg 145 and Glu 270 be? (b) Explain how the two amino acid residues can catalyze a reaction occurring in the space of a few angstroms
Draw a Haworth projection and Fischer projection for a methyl α-D-mannopyranoside (methyl α-D-mannoside). Label the anomeric carbon and the glycosidic bond.
(a) As the pH changes from 9.0 to 5.0, how does the concentration of H+ (protons) change? (b) Describe how the charge of some amino groups in a protein might differ at pH 9.0 and pH 5.0. (c) Describe how the charge of some carboxyl groups in a protein might differ at pH 9.0 and pH 5.0. (d) Given your answers to parts (b) and (c), what kind of intramolecular interactions in beta-galactosidase are most likely to be affected by a change in pH from 9.0 to 5.0? (e) Could the interactions you mention in part (d) affect the catalytic activity of beta-galactosidase?

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