Match amino to possible function or role in a membrane protein. (Choose the bestanswer)Interact with lipid tails[ Choose ][Choose ]CysteineInteract with Na ion within a poreHistidineMethionineProlineLeucineInteract with phosphates of ATP in aLysineTryptophanbinding pocketGlutamateShow fluorescence in response to a[ Choose ]conformational change upon ligandbindingForm a disulfide to stabilize a tertiary[ Choose ]structureBind to the iron within a heme group[ Choose ]to coordinate oxygen sensingEnd an alpha helix leading to a coiled[Choose ]region>>>>

Amino acids are the compound of C, H, O, N and S. An amino acid consists of a carboxylic group, an…

Answered: Match amino to possible function or…

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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Multifunctional protein kinases O phosphorylate various targets with the correct consensus sequence carry out phosphorylation as well as sulfonation reactions O remove phosphates through hydrolysis O have a very specific target that they phosphorylate conserve energy in the form of ATP from the degradation of proteins
6
The majority of amino acid residues found in the portion of a beta-barrel in contact with the transported solute are O hydrophobic O cyclic O hydrophilic O aromatic Previous Nort
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
What are some of the interactions made between ATP and the kinase? Can you please describe bonds that the protein makes with (a) the phosphate groups, (b) the sugar, and (c) the adenine base? Please don't just copy answers from google.. I already read most of em.. :(
1. The CFTR protein is a chloride channel in the cell membrane. Use your understanding of the biochemical properties/categories of amino acids and how they interact with membrane phospholipids to predict the distribution of charged/polar, and non-polar amino acids within the domains of CFTR listed below. Consider one category to include the charged amino acids and the polar amino acids and the other category to include the non-polar amino acids. For each domain, predict which category of amino acids is likely to be most abundant. Also, explain the rationale behind your prediction. Protein domain Prediction (Charged/Polar or Non-Polar amino acids?) Explanation for prediction TMD1 and TMD2 (transmembrane domains, parts 1-12) ECLs and ICLs (extracellular and intracellular loops) NBD1 and NBD2 R
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
The role of GTP hydrolysis in actin polymerization is similar to the role of ATP hydrolysis in tubulin polymerization: both serve to weaken the bonds in the polymer and thereby promote depolymerization. Is that true or false? why?

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