In an alpha helical protein that spans a cell membrane,the membrane whilewould likely be associated with the aqueous environmentO His; Ser; ThrCIle; Asn; GluTyr; Glu; GlyTrp: Asn; Ala(Ctrl)would likely be in the center ofwould likely be associated with the polar head groups and

The amino acids are classified as polar and non-polar. The integral membrane proteins are…

Answered: would likely be in the center of would…

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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Proteins involved in transport of molecules or ions into orout of cells are found in the membranes of all cells. They areclassified as transmembrane proteins because some regionsare embedded within the lipid bilayer, whereas other regionsprotrude into the cytoplasm or outside the cell. Review theclassification of amino acids based on the properties of theirR groups. What type of amino acids would you expect tofind in the regions of the proteins embedded within themembrane? What type of amino acids would you expect tofind on the surface of the regions in the cytoplasm or thatprotrude outside the cell?
Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…
When a protein is folded in aqueous solution, some residues are driven inside to form a “hydrophobic core” which is far away from the water molecule. Which pair of the following residues are likely to be in the “hydrophobic core”? a. Gln and His b. Thr and Val c. Asp and Arg d. Ser and Tyr e. Ile and Leu
What is the difference between the protein chain (amino acids) of proteins that end up in the ER lumen and that end up in the ER membrane?
Describe the two types of secondary structure apolypeptide can attain. Which proteins can achievequaternary structure? Which protein structure(s) are alteredby denaturation?
Although proteins rarely if ever flip-flop across a membrane, the distribution of membrane lipids between the membrane leaflets is not absolute except for glycolipids. Why are glycosylated lipids less likely to flip-flop?
Researchers have discovered a new membrane protein that has three transmembrane domain αhelixes that span the lipid bilayer.a. If the lipid bilayer is 30 Å thick, what is the smallest number of amino acid residues thatcan be in each α-helixes for them to be long enough to span the bilayer?
Aquaporins are proteins embedded in the plasmamembrane that allow water molecules to move betweenthe extracellular matrix and the intracellular space.Based on its function and location, describe the keyfeatures of the protein’s shape and the chemicalcharacteristics of its amino acids.
It is observed that as temperature is increased, most protein molecules gofrom their defined, folded state into a random-coil, denatured state thatexposes more hydrophobic surface area than is exposed in the folded state.(a) Given what you have learned so far about ΔH and ΔS, explain why thisis reasonable. (b) Sometimes, however, proteins denature as temperature is decreased.How might this be explained?
you have isolated a new protein called STICKY. you can predict from comparisons with other known proteins that STICKY contains bHLH domain. Predict the function of STICKY and rationale forthe importnce of these domains in sticky function.
A transmembrane protein in the plasma membrane is glycosylated attwo sites in the polypeptide sequence. Where in this protein would youexpect these two sites to be found?a. in transmembrane segmentsb. in hydrophilic regions that project into the extracellular environmentc. in hydrophilic regions that project into the cytosold. could be anywheree. b and c only
Many proteins contain one or more motifs built from particular combinations of secondary structure. Describe the three common structural motifs and describe some of the general functions of protein domains on the extracellular membrane surface, within the membrane, or on the cytosolic face of the membrane. Whatr are the biological activities of proteins are affected by chemical modifications.

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would likely be in the center of would likely be associated with the polar head groups and In an alpha helical protein that spans a cell membrane,. the membrane while would likely be associated with the aqueous environment His; Ser; Thr Ile; Asn; Glu Tyr; Glu; Glx. Trp: Asn; Ala (Ctrl) -