Question 23 QUESTION 23The complete denaturation of a protein that is made of only a single polypeptide chain leads to the loss ofstructure.O a primary and secondaryOb. secondaryOc tertiaryO d. secondary and tertiaryQUESTION 24alpha-helix structure:O a. are stabilized by hydrogen bonding between the R-groups of the two adjutant amino acidsO b. are favored by amino acid sequences that contain the repeating pattern, Gly-Ala-GlyOc are stabilized by hydrogen bonding between carbonyl and amide groups of the main chainO d. are a form of quaternary structureO e. are composed of only 2-5 amino acids that must be of the opposite polarityQUESTION 25Which bond in a polypeptide chain has partial double bond character? (C' = carbonyl carbon)O Ca-HO c-cON-CaO ca-CO c-Nlick Save All Answers to save all answers.7 he ayedStudet SppotMyCourses

Denaturation is a process in which proteins lose their native conformation i.e. normal, biologically…

Answered: QUESTION 23 structure. The complete…

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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QUESTION NO. 1Targeting a protein to be degraded within proteasomes usually requires ubiquitin. In the function of ubiquitin all of the following are true except: A. ATP is required for activation of ubiquicin. B. a peptide bond forms between the carboxyl terminal of ubiquitin and an ε-amino group of a lysine . C. linkage of a protein to ubiquitin does not always mark it for degradation. D. the N-terminal amino acid is one determinant of selection for degradation. E. ATP is required by the enzyme that transfers the ubiquitin to the protein to be degraded QUESTION NO. 2Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except. A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition…
Question 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH
Question 1: Your research project is concerned with the expression and purification of a protein called aldehyde dehydrogenase. Describe in detail all steps required from gene amplification to characterisation of the purified protein.
QUESTION 12 The leucine zipper domain of transcription factors is not involved in DNA recognition but rather in facilitating dimerization. Given the chemical properties of the amino acid leucine, dimerization of transcription factors via this domain by (select the correct option). Facilitating hydrogen bonding with the aqueous environment. Chelation of bivalent ions such as Zn2+. Formation of coiled-coils through hydrophobic non-covalent interactions between evenly spaced Leu residues in alpha-helical domains. Physically connecting the two transcription factor subunits through unstructured loops.
QUESTION NO.1which of the following are chemical characteristics of monosaccharides? A. They contain multiple hydroxyl groupsB. they contain an aldehyde or ketone group C. They contain a branching carbon backbone D. They contain a carbon-carbon double bond E. Every carbon in a monosaccharide is fully reduced F. Every carbon in a monosaccharide is a chiral centerQUESTION NO.2 glucose absorption is hindered by _________ deficiency A. Retinol B. Thiamine C. Potassium D. Sodium E. Ascorbic acid F. Calciferol QUESTION NO.3 phospholipids is made primarily from A. L-glycerol 1-phosphate B. L-glycerol 3-phosphate C. D-glycerol 3-phosphate D. -glycerol 1-phosphate E. sn-glycerol 1-phosphate F. sn-glycerol 3-phosphate
Question 15 Activities found in the rough ER and its functions include the folllowing EXCEPT provides a membrane binding site for the RNA with signal a signal sequence facilitates post-translational modifications allows the entry of polypeptides that will undergo glycosylation provides a membrane scaffold for binding of ribosomes for protein synthesis
Question 1: tRNA and amino acyl tRNA synthetases Part g: What chemical and structural characters are shared by the amino acids Ile, Val and Met? Part h: What enzyme attaches Ile to tRNA? Part i: Compare the frequency of the correct Ile entering the active site and the frequency of an incorrect amino acid entering the active site of this enzyme. Be specific with numbers. Part j: Compare the frequency of the correct tRNA(Ile) entering the active site and the frequency of an incorrect tRNA entering the active site of this enzyme. Be specific with numbers. Part k: Apply the Entropy change formula and multiply by T = 303 K (30 C) to determine the energetic cost of accurately attaching Ile to its cognate tRNA(Ile). Part l: Is there enough energy in the chemical transformation of ATP → AMP + 2Pi to pay this information cost?
question 24 DNA is a hereditary molecular that is composed of A Deoxyribose,phosphate, and nitrogen bases B Deoxyribose,a pentose, and nucleic acids C Sugar,proteins and thymine D Adenine, phosphate, and ribose
QUESTION NO. 1 Fragile X syndrome is a common form of inherited mental retardation. The mutation in the disease allows the increase of a CGG repeat in a particular gene from a normal of about 30 repeats to 200-1000 repeats. This repeat is normally found in the 5' untranslated region of a gene for the protein FMR1. FMR1 might be involved in the translation of brain-specific mRNAs during brain development. The consequence of the very large number of CGG repeats in the DNA is extensive methylation of the entire promoter region of the FMR1 gene. Methylation of bases in DNA usually A. facilitates the binding of transcription factors to the DNA. B. makes a difference in activity only if it occurs in an enhancer region. C. prevents chromatin from unwinding. D. inactivates DNA for transcription. E. results in increased production of the produce of whatever gene is methylated.QUESTION NO. 2 The best definition of an endonuclease is that it hydrolyzes A. nucleotide from…
Question 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSN
Question 1: tRNA and amino acyl tRNA synthetases Part a: How many codons encode the amino acid Isoleucine (Ile, I)? Part b: How many codons encode the amino acid Valine (Val, V)? Part c: How many codons encode the amino acid Methionine (Met, M)? Part d: How many tRNAs decode the Ile codons? Part e: How many tRNAs decode the Val codons? Part f: How many tRNAs decode the Met codon?
QUESTION NO. 1 Cystic fibrosis is a frequent generic disease of Caucasians. The CF gene codes for a protein called the cystic fibrosis transmembrane conductance regulator (CFTR) which functions as a cAMP-regulated chloride channel. The protein has two membrane-spanning domains, two domains that interact with ATP, and one regulatory domain. The most common defect is in the gene for one of the ATP binding domains. The result is a protein that does not fold correctly in the endoplasmic reticulum, is not properly glycosylated, and is nor transported to the cell surface. Rather, it is degraded in the cytosol within proteasomes. Drugs that foster chaperone interaction with the mutant protein are a potential therapeutic approach. Chaperones A. are always required to direct the folding of proteins. B. when bound to protein increase the rate of protein degradation. C. usually bind to strongly hydrophilic regions of unfolded proteins. D. sometimes maintain proteins in an…

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QUESTION 23 structure. The complete denaturation of a protein that is made of only a single polypeptide chain leads to the loss of primary and secondary Ob secondary O tertiary Od secondary and tertiary