Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 26, Problem 38P
Interpretation Introduction
Interpretation:
The reason for the modification of proteins by the covalent linking of a farnesyl or a geranylgeranyl unit to the carboxyl-terminal cysteine residue should be determined.
Concept introduction:
Phospholipids are the basic constituent of all cell membranes. They usually form lipid bilayers. The structure of a phospholipid molecule has a tail made up of two hydrophobic fatty acid and a hydrophilic head comprising of a phosphate group.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
resting state of the protein, the Lys 216 Schiff base has pKa = 9.5 and Asp 85 has pKa = 3.5. When the conformational change occurs, the proton that was on the Schiff base moves to Asp 85. This should tell you that one or both of these two pKas
changed with the conformational change. How does the pKa of Asp 85 compare with the pKa of the Lys 216 Schiff base after the conformational change?
cip sequence rule in ephedrine
Upload a drawing of Gly-Met-Asn-Glu-His
Label the alpha carbons
Label the R groups as hydrophobic or hydrophilic
Label the acidic and basic R-groups
Label the peptide bonds
Label the N terminus and the C terminus
Chapter 26 Solutions
Biochemistry
Ch. 26 - Prob. 1PCh. 26 - Prob. 2PCh. 26 - Prob. 3PCh. 26 - Prob. 4PCh. 26 - Prob. 5PCh. 26 - Prob. 6PCh. 26 - Prob. 7PCh. 26 - Prob. 8PCh. 26 - Prob. 9PCh. 26 - Prob. 10P
Ch. 26 - Prob. 11PCh. 26 - Prob. 12PCh. 26 - Prob. 13PCh. 26 - Prob. 14PCh. 26 - Prob. 15PCh. 26 - Prob. 16PCh. 26 - Prob. 17PCh. 26 - Prob. 18PCh. 26 - Prob. 19PCh. 26 - Prob. 20PCh. 26 - Prob. 21PCh. 26 - Prob. 22PCh. 26 - Prob. 23PCh. 26 - Prob. 24PCh. 26 - Prob. 25PCh. 26 - Prob. 26PCh. 26 - Prob. 27PCh. 26 - Prob. 28PCh. 26 - Prob. 29PCh. 26 - Prob. 30PCh. 26 - Prob. 31PCh. 26 - Prob. 32PCh. 26 - Prob. 33PCh. 26 - Prob. 34PCh. 26 - Prob. 35PCh. 26 - Prob. 36PCh. 26 - Prob. 37PCh. 26 - Prob. 38PCh. 26 - Prob. 39PCh. 26 - Prob. 40PCh. 26 - Prob. 41PCh. 26 - Prob. 42PCh. 26 - Prob. 43PCh. 26 - Prob. 44PCh. 26 - Prob. 45PCh. 26 - Prob. 46PCh. 26 - Prob. 47P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- In α-helices - what is the length of the hydrogen bonds between: TYR41H and GLU37O ALA39H and MET35O GLU38H and ILE34O THR36H and ARG32O. ARG32H and TYR28Oarrow_forwardReposting - What would the tertiary structure of the dipeptide Asp-Ser be if it was made into a polypeptide chain? (Would it form a beta pleated sheet, an alpha helix, etc) Why would it do this? What properties of this polypeptide causes this? This sub part still needs to be solved - What would the tertiary structure of Pro-ala and Glycl-L-alanine be?arrow_forwardNo plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. Explain the formation of thioether-linked prenyl anchor proteins. Explain the structure of caveolae.arrow_forward
- Hydropathy plot analysis of your protein of interest reveals a single, prominent hydrophobic peak. However, you later discover that this protein is soluble and not membrane associated. Explain how the hydropathy plot may have been misleading.arrow_forwardBeta ( ? ) sheets are a type of secondary structure in proteins. A segment of a single chain in an antiparallel ? sheet has a length of 80.5 Å . How many residues are in this segment?arrow_forwardChoose if it's true or false Different from RNA since in the latter the internucleotide linkages are between C-2’ and C-5’ A long chain polymer in which the internucleotide linkages are of the diester type between C-3’ and C-5’ Usually present in tissues as a nucleoprotein and cannot be separated from its protein component Hydrolyzed by weak alkali (pH 9 to 100°C)arrow_forward
- Hi - I have the following as a question in my biochemistry course and I am just lost on where to start. Thanks! Cyt cb562 will form a tetramer in the presence of Zn+2 or in the absence of Zn+2, it will form a trimer. For both the tetramer and the trimer, suggest the identity of three different amino acids that could be on the interface. Explain how your selections facilitate these interactions.arrow_forwarddon't copy 6. A protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.arrow_forwardCompare and contrast structural features of collagen and α-keratin (OK to do this as a list or table comparing/contrasting 3-4 points, e.g. type of helices, noncovalent and covalent interactions between helices, favored residues). Can you please help?arrow_forward
- A cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.arrow_forwardWhich intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.arrow_forwardHuman hemoglobin as a tetrameric protein of about 64.5KDa consists of 2 beta chains. Calculate the number of amino acides present in the alpha chainsarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Anaerobic Respiration; Author: Bozeman Science;https://www.youtube.com/watch?v=cDC29iBxb3w;License: Standard YouTube License, CC-BY