Which is the best explanation of why kinesin doesn't bind covalently to its structural proteintracks?O Energy gained from ATP hydrolysis would go towards powering bond breaking instead of movement.O Kinesins do not contain any chemical constituents capable of making covalent bonds with their structuraltracks.O These stronger non-covalent interaction's, versus the weaker covalent ones, are required to keep kinesin onits structural protein tracks.O It is important to prevent kinesins from making any contact with their structural tracks in order to allowcargo transport.

Kinesins are motor proteins responsible for transporting cellular cargo along microtubules within…

Answered: Which is the best explanation of why…

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

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.
Histidine is an amino acid with three ionizable groups, one of which has a pKa of 6.0. This group, whenprotonated, has a positive charge. If this ionizable group, within a protein, forms an ionic interaction with anegatively charged group, what would you predict would happen to the pKa of the histidine ionizable group?A. IncreaseB. DecreaseC. Stay the same
Previously Protein A and 5mM of ligand X were combined in a neutral solution and 36% of Protein A was ligand bound. Now Protein A and ligand X are combined in an acidic solution. You now find that when there’s a 4 mM concentration of free ligand X, 45% of the protein is bound to ligand. How does a change in pH affect protein A’s affinity for ligand X? a. Protein A has a higher affinity for ligand X in acidic environments b. Protein A has a lower affinity for ligand X in acidic environments c. The solution pH does not affect the affinity of protein A for ligand X. d. The solution pH does not affect the affinity of a protein for a ligand.
What is the most consistently (i.e. found in every case) energetically unfavorable aspect of protein folding? Does it involve ΔS or ΔH? And what is the most consistently favorable aspect? Again, ΔS or ΔH?
..You have isolated a new protein called STICKY. You can predict from comparisons with other known proteins thatSTICKY contains a bHLH domain.Predict the function of STICKY and rationale for the importance of these domains in STICKY function.. ..
In the tertiary structure of a protein, which pair of amino acid side chains would be most likely to participate in hydrophobic interactions? Asn/lys ser/cys gln/tyr val/thr phe/lêu
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
When an amino acid's side chain, such as aspartic acid, has a pKa, that pKa is not the same if the amino acid occurs on the interior of a protein. Why would the pKa of a side chain of an Asp occuring on the inside of a protein be different from an Asp on the outside of a protein?
What molecule allowed our target protein to elute off our affinity column? O a. lysozyme O b. BSA O c. imidazole O d. Laemmli O e. PMSF What information can isoelectric focusing provide about a protein? choose one or more: a. its pl b. its degree of purity c. its Km d. its molecular weight
Which of the following statements are correct about protein folding (select all that appy)? A. Protein folding is a very slow process with most proteins requiring >30 min to go from unfolded to native conformation B. The mature two-chain form of insulin spontaneously folds into the native conformation C. A sharp transition in the presence of denaturants (See Figue 8.1) suggests the protein folds without intermediates D. Proteins randomly sample each possible conformation before arriving final native state E. Proteins with disulfide bridges tend not follow a simple two-state folding mechanism.
For this homework it’s a protein but I am stuck because it asks This molecule can have _____ levels of structure And then it asks What level of structure is shown in this protein marcromolecule Then asks if I add another chain to this molecule what level of structure will that be? What are the other levels of structure it can have and how are they formed
What would be the molecular sequence of the amino acid chain asp-leu-leu? (i.e. draw the whole sequence out as molecules joined together)

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