BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 24, Problem 14P
Interpretation Introduction
Interpretation:
Common cofactor used by all aminotransferases should be determined.
Concept introduction:
Aminotransferases are also termed as transaminases. The function of these enzymes is to catalyze the reaction between an amino acid and an alpha-keto acid. This reaction and the enzyme is required during the synthesis of amino acids, which are the basic units of the proteins.
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an inorganic ion. Such as metal ion, that improves the fit of an enzyme with its substrate is a(n)?
- Keto counterparts. Name the a-ketoacida-ketoacid that is formed by
the transamination of each of the following amino acids: Co,
a. Alanine
b. Leucine
c. Aspartate
d. Phenylalanine
e. Glutamate
f. Tyrosine
. A nervous polecat. Pyrrolysine (Pyl, O) and Selenocysteine (Sec, U) are two uncommon amino acids.
Knowing that these amino acids exists, translate the following amino acid sequence into one – letter code: Thr
– Trp – Ile – Thr – Cys – His – Tyr – Leu – Ile – Thr – Thr – Ile – Glu – Phe – Glu – Arg – Arg – Glu – Thr – Ala
– Arg – Glu – Asn – Thr – Tyr – Pyl – Sec – Met – Ala – Leu – Phe – Pyl – Tyr.
Chapter 24 Solutions
BIOCHEMISTRY-ACHIEVE (1 TERM)
Ch. 24 - Prob. 1PCh. 24 - Prob. 2PCh. 24 - Prob. 3PCh. 24 - Prob. 4PCh. 24 - Prob. 5PCh. 24 - Prob. 6PCh. 24 - Prob. 7PCh. 24 - Prob. 8PCh. 24 - Prob. 9PCh. 24 - Prob. 10P
Ch. 24 - Prob. 11PCh. 24 - Prob. 12PCh. 24 - Prob. 13PCh. 24 - Prob. 14PCh. 24 - Prob. 15PCh. 24 - Prob. 16PCh. 24 - Prob. 17PCh. 24 - Prob. 18PCh. 24 - Prob. 19PCh. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - Prob. 25PCh. 24 - Prob. 26PCh. 24 - Prob. 27PCh. 24 - Prob. 28PCh. 24 - Prob. 29PCh. 24 - Prob. 30PCh. 24 - Prob. 31PCh. 24 - Prob. 32PCh. 24 - Prob. 33PCh. 24 - Prob. 34PCh. 24 - Prob. 35PCh. 24 - Prob. 36PCh. 24 - Prob. 37PCh. 24 - Prob. 38PCh. 24 - Prob. 39PCh. 24 - Prob. 40P
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Similar questions
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- No plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. Explain the formation of thioether-linked prenyl anchor proteins. Explain the structure of caveolae.arrow_forwardNeed help, please. Not too sure why my answer is incorrect. Please show all steps/work.arrow_forwardNeed help, please. Not too sure why my answer is incorrect. Please show all steps/work.arrow_forward
- Need help, please. Not too sure why my answer is incorrect. Please show all steps/work.arrow_forwardNeed help. (a) Two ligands bind to the same site of a protein. However, when examined by ITC, for one of the ligands heat needs to be added to the system to maintain constant temperature, whereas for the other ligand, heat must be removed. Why is this the case?arrow_forwardRequired partner. Aminotransferases require which of the following cofactors: a. NAD+/NADP+NAD+/NADP+ b. Pyridoxal phosphate c. Thiamine pyrophosphate d. Biopterinarrow_forward
- Beta folding. Parallel and antiparallel beta folding sheets (be able to draw). Beta loops. Examples of proteins formed mainly by this structure.arrow_forwardI. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4arrow_forwardPlease ASAP. Thank you. How does the mutation change/affect the structure of the Hb heterotetramer (ie how is quaternary protein structure affected)?arrow_forward
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