Question 24 QUESTION 24alpha-helix structure:O a. are stabilized by hydrogen bonding between the R-groups of the two adjutant amino acidsOb. 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 chainOd. are a form of quaternary structureOe.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 Co-CO c-NQUESTION 26Consider the following properties of the listed proteins A, B and C.ProteinplAffinityfor glucoseYesNoNolick Save All Answers to save all answers.Q O!17 edShudent SupportMyCourses

The α helix is stabilized by hydrogen bonds between an amide hydrogen of one amino acid and a…

Answered: QUESTION 24 alpha-helix structure: are…

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:- Alpha-endorphin is a peptide with an amino acid sequence of YGGFMTSEKSQTPLVT. How many charges does it have at pH 7?
Question one parts A though E a. True / False: Guanine to cytosine intermolecular interactions (hydrogen bonding) is stronger than adenine to thymine. b. What peptide would be made from the following DNA sequence? 5'ATCCCGGGTACTCACTCCCAT3' Start-Gly-Pro-Stop Start-Gly-Ser-Pro-Val-Arg-Val Start-Gly-Gly-Thr-lle-Arg Start-Arg-Arg-Gly-Gly c. Starting from the MRNA strand below - what peptide would be produced? Remember your start and stop codons...5'CCAUGCGGCAUACCAAAUUACUAAACUAGC3' Start-Arg-His-Thr-Lys-Leu-Leu-Asn-Stop Start-Asn-Leu-Leu-Lys-Thr-His-Arg-Stop Start-Arg-Lys-Leu-Asn-Stop Pro-Met-Arg-His-Leu-Leu-Asn d. Which type of RNA comprises over 80% of total cellular RNA? ribosomal RNA Messenger RNA Transfer RNA e. True / False - All of the DNA nucleotides are attached to the deoxyribose in the BETA configuration (at the anomeric carbon of the sugar). B (Ctrl) -
Time remaining: 00:08:55 Chemistry Consider a peptide with the following amino acid sequence: H2N-ASENHLDGCPYTKSRG-COOH Analyze the predominate protonation state and thus dominate charge (+1, 0, -1) of the residues in this peptide at pH 3, 6, and 10 by filling in the table below, identifying the relevant pKa appropriate for each residue. (Note that choice of pKa and its. application will be graded independently; e.g., if you can choose the wrong pKa but apply it correctly, you will lose points only for the pKa.) AA Residue pKa Charge pH 3 Charge pH 6 Charge pH 10 A S E N H L D G C P Y T K S R G
QUESTION S Amino acid monomers are grouped into three categories based on their "R" group around the alpha carbon. Which pairing most accurately depicts the reason for the "R" group category? O Polar uncharged R group amino acids have functional groups that are strongly electronegative. O Non polar R group amino acids have hydrocarbon functional groups such as methane. O Polar charged R group amino acids have functional carboxyl and amino functional groups
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 A test protein contains the following 4 ratios of its amino acid content (mg/g) vs the amino acid content in the adult reference pattern (mg/g): histidine 0.80, isoleucine 0.62, methionine + cysteine 0.50, tryptophan 0.60. What is the test protein's amino acid score (AAS)? O 0.80 O 0.62 O 0.60 O 0.50 O Cannot calculate given this information QUESTION Based on question 25, what is/are the limiting amino acid(s) in this test protein? O Histidine O Isoleucine O Methionine + cysteine O Tryptophan O Cannot calculate given this information QUESTION The test protein referred to in question 25 and 26 has a digestibility of 90%. What is the protein digestibility-corrected amino acid score (PDCAAS)? O 0.80 O 0.56 O 0.50 O 0.45 O Cannot calculate given this information
P Question 16 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 O D. Inefficient folding by chaperone proteins O E. All of the above are correct answers
Question What is the net charge for the following peptide at pH = 1? Ser-Trp-Arg-Gln-Glu-His-Lys-Asp
Question What is the net charge for the following peptide at pH = 7 (neutral pH)? Ser-Trp-Arg-Gln-Glu-His-Lys-Asp
QUESTION 03 - Regarding the amino acid arginine, answer the following questions: (Data: pka a) NH₂ HN ΝΗ (-COOH) =2,17;pka Arginina (-NH3) NH₂ =9,04;pka OH Explain using resonance structures why, when the arginine side chain isprotonated nitrogen, from the guanidino group, which a double bond is the one that accepts the proton. = 12.48) Discuss why the form in which arginine was written would not be found in solution, considering opH=physiological (7,3).
Question: 1. Identify the amino acids in this peptide 2. Which amino acid sidechains are protonated at physiological pH 3. What is the overall charge of this peptide H₂N O NH₂ IZ ZI O OH IZ OH OH
Question for protein crystallography- 1. While performing a routine protein crystallization screening, you observe that one of your well drops has doubled in size compared to the remaining wells. Note: the drop in question was set up by taking 1 µL of the protein solution (10 mg/mL LDH in 20 mM TRIS pH 7.5, 0.5 M NaCl and 10% PEG 4000K) and adding it to 1 µL of the crystallization solution (10% PEG 4000K, 50 mM NaCl and 20 mM TRIS pH 8.0). Why did this drop grow larger in size compared to when you initially set it up?

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