GLUT1 is a type III integral membrane protein with 12 amphipathic helices that span the cellmembrane. Which amino acid side chains from the following amino acid sequence are most likely toform the hydrophobic (non-polar) face of an amphipathic alpha helix?-Ser-Leu-Val-Thr-Asn-Phe-Ile-0941Select one:54W7263DRO10:00 GLUT1 is a type III integral membrane protein with 12 amphipathic helices that span the cellmembrane. Which amino acid side chains from the following amino acid sequence are most likely toform the hydrophobic (non-polar) face of an amphipathic alpha helix?-Ser-Leu-Val-Thr-Asn-Phe-Ile-0941Select one:54W7263DRO10:00

GLUT1 refers to glucose transporter 1 protein, which plays a crucial role in transporting glucose…

Answered: GLUT1 is a type III integral membrane…

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

Glutamine is an amino acid that has -CH₂-CH2-CO-NH₂ as its R group. The R group of the amino acid isoleucine is -CH2-CH-(CH3)2. If these amino acids were in a globular protein in aqueous solution, where would they most likely be? O Both glutamine and isoleucine would be in the interior and on the exterior of the globular protein. O Glutamine would be in the interior, and isoleucine would be on the exterior of the globular protein. O There isn't enough information O Both glutamine and isoleucine would be on the exterior of the globular protein. O Isoleucine would be in the interior, and glutamine would be on the exterior of the globular protein.
Draw the peptide formed between asparagine and histidine. H,N- -CH-C-OH H,N-CH-ċ-OH ČH2 ČH, N° NH2 -NH +
Consider protein folding that results when the following components interact: Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.
If you were given the abbreviations for 4-6 amino acids, could you draw the polypeptide chain AND determine its isoelectric point? Do this for the amino acid Asp-Arg-Val-Tyr-Ile
Peptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE Which of these peptides would be most likely to be found as an a helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an a helix in a transmembrane protein? Which would be least likely to form an a helix of any kind? Briefly explain your answers.
Which amino acid sequence will form part of which protein structure, and why? Sequence 1: Ser-Phe-Gln-Val-Lys-Leu-His-Tyr-Asp-Val Sequence 2: Glu-Tyr-Leu-Asn-Phe-Ala-Gln-Val-Leu-Arg __Amphipathic beta strand __ Amphipathic alpha helix

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GLUT1 is a type III integral membrane protein with 12 amphipathic helices that span the cell membrane. Which amino acid side chains from the following amino acid sequence are most likely to form the hydrophobic (non-polar) face of an amphipathic alpha helix? -Ser-Leu-Val-Thr-Asn-Phe-Ile-