Two peptides have almost the exact same primary structure, except that one has about 10 fewer amino acids at the amino-terminus (N-terminus) of the protein. What is a possible explanation for the protein that is missing those 10 amino acids? O A. An alternative Poly-A tail addition site O B. Leaky scanning occurred O.Differential glycosylation of the protein D. Inefficient folding by chaperone proteins O E. All of the above are correct answers

Two peptides have almost the exact same primary structure, except that one has about 10 fewer amino acids at the amino-terminus (N-terminus) of the protein. What is a possible explanation for the protein that is missing those 10 amino acids? O A. An alternative Poly-A tail addition site O B. Leaky scanning occurred O.Differential glycosylation of the protein D. Inefficient folding by chaperone proteins O E. All of the above are correct answers

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Proteins can be precipitated out of aqueous solution bythe addition of an electrolyte; this process is called “saltingout” the protein. (a) Do you think that all proteins wouldbe precipitated out to the same extent by the same concentrationof the same electrolyte? (b) If a protein has beensalted out, are the protein–protein interactions stronger orweaker than they were before the electrolyte was added?
What following statement is TRUE concerning motifs and domains? a) Both motifs and domains are independently stable. b) Domains undergo dynamic individual changes that affect the entire protein c) B-a-ß loops, B barrels, and helix-turn-helix structure are types of domains d) Motifs and domains are part of secondary structural elements e) Ab initio computations predict motif folds accurately a majority of the time My guess is B.
1.a.If this molecule was the side chain of an amino acid, in a protein, what tertiary structure stabilizers could be present? b.Make a key and use color to highlight what part of you structure can be stabilized in each manner?
An unspecified protein contains a 15-residue long α-helix with the following sequence: WEANIKQRLSTMGEYKQCHANG a. How many full turns are there in this α-helix? b. What is the length of the helix (in Angstroms) in the direction of the helix axis? c. How many hydrogen bonding interactions would be there in this α-helix? d. If it was a 310 helix instead with a helical pitch of 6 Å, is it long enough to span the 30 Å bilayer? Calculate and explain.
Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys Cys
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?
2. A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U). Show that the ligand stabilizes the protein and calculate by how much (ΔΔGfold = ?). Please help me find out deltadelta G fold.
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
If Kd= 100 nM, [RNA] = 10 nM, and [protein] = 1 uM a) What fraction of RNA is bound? b) What fraction of protein is bound? c) What is the concentration of the protein:RNA complex? d) Is it reasonable to assume that total protein = free protein? e) Is it reasonable to assume that total RNA = free RNA?
SDS-PAGE gels are used to study changes in protein primary structure. Which of the following statements about SDS-PAGE gels is correct? A. The negatively charged proteins will move towards the negatively charged electrode in the SDS-Page chamber B. A detergent is needed to disrupt protein secondary, tertiary, and quaternary structure before a gel can be run C. No "stains" or other treatments are needed to "see" the protein bands on a gel D. Long polypeptides move a further distance from the loading well in a SDS-PAGE gel than short polypeptides
Explain how tandem mass spectroscopy is used to determinethe sequence of a peptide. Once a peptide sequence is known,how is this information used to determine the sequence of theentire protein?
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.