Which type of motifs/folds are found in the protein shown belowCoiled-coilO EF HandO HorseshoeO RossmannO Jelly rollO Greek keyO Alpha/beta barrelO Beta barrelO Beta sandwichOZinc finger

The final products of the expression, "the proteins" attain higher folding confirmation of…

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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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What part of the structure is represented by the second chain having the order Asp- Asp-Ser-Val? "B-bridge" Nb Na "B-bridge" O Quaternary structure
Changing one amino acid within a protein sequence from a tryptophan to a stop codon would be best classified as Amino acids groups Group Characteristics Names Ala, Val, Leu, Ile, Pro, Phe Trp, Met Ala: A Leu: L non-polar hydrophobic Arg: R Asn: N Lys: K Met: M Asp: D Cys: C Gly: G polar hydrophilic (non-charged) Gly , Ser, Thr, Cys, Tyr, Asn Gln Phe: F Pro: P Ser: S acidic negatively charged Asp, Glu Glu: E Gln: Q Thr: T His: H lle: I Trp: W Туr: Y Val: V basic positively charged Lys, Arg, His A) Conservative missense O B) Nonsense O C) Neutral O D) Non-conservative missense
A polypeptide is digested with trypsin, and the resulting segments are sequenced: Val-Gly Ala-Ala-Gly-Leu-Trp-Arg Arg-Asp-Pro-Gly-Lue-Met-Val-Leu-Tyr-Ala-Ala-Asp-Glu-Lys And the following fragments are produced by chymotrypsin fragmentation: Ala-Ala-Gly-Leu-Trp Arg-Arg-Asp-Pro-Gly-Leu- Met-Val-Leu-Tyr Ala-Ala-Asp-Glu-Lys-Val-Gly What is the sequence of the whole original polypeptide? (Recall that trypsin cleaves a polypeptide backbone at the C-terminal side of Arg or Lys residues, whereas chymotrypsin cleaves after aromatic amino acid residues).
A polypeptide is digested with trypsin, and the resulting segments are sequenced: Val-Gly Ala-Ala-Gly-Leu-Trp-Arg Arg-Asp-Pro-Gly-Lue-Met-Val-Leu-Tyr-Ala-Ala-Asp-Glu-Lys And the following fragments are produced by chymotrypsin fragmentation: Ala-Ala-Gly-Leu-Trp Arg-Arg-Asp-Pro-Gly-Leu- Met-Val-Leu-Tyr Ala-Ala-Asp-Glu-Lys-Val-Gly What is the sequence of the whole original polypeptide?
Draw beta sheet with backbone hydrogen bonds, is this structure on the interior or exterior of the protein and why? Region 1: -Ser-Thr-Glu-His- Region 2: -Asp-Tyr-Lys-Asn
Name the protein structural element shown in yellow in the figure: B-barrel reverse turn disordered region a-helix parallel ß sheet
Translate the following DNA sequence into amino acids 5'ATAGTACCGCAAATTTATCGCT3 O met-ala-phe-lys-stop O met-ala-phe-lys- met-tyr-his-gly-val-stop-met-gly O met-ala-ser-gly-thr-stop O tyr-his gly-val-stop-met-ly O ala-phe-lys stop
have simply replaced hydrogen bonds with water in the unfolded protein, yet they critical to stability of the folded protein. Why?
Which of the following best describes how the secondary structure of a protein is formed? A B с D O=U a-helix H O=C N-H R-C-H C=0 H-N H-C-R O=C N-H R-C-H C=O H-N O-C N-H R-C-H C=O H-N N-H 0= H-C-R H-N C=O R-C-4 N-H O=C H-C-R 4-1 Ç=O R-C-H N-H 0=C H-C-R (=O R-C-H B-pleated sheet ionic bonds between the R groups of the polypeptide amino acids -Uh hydrogen bonds between the carboxyl and amino groups of non-adjacent amino acids covalent bonds between the carboxyl and amino groups of adjacent amino acids hydrogen bonds between the R groups of the polypeptide amino acids
Which of the following polypeptides would be most likely to form an a helix? Explain your answer. Cys-Arg-Ala-Gly-Asn-Arg-Lys-Glu-Thr-Tyr-Ile-Val-LeuSer-Glu-Asp-Asn-Phe-Gly-Ala-Pro-Lys-Ser-Ile-Leu-TrpGln-Lys-Ala-Ser-Val-Glu-Met-Ala-Val-Arg-Asn-Ser-Gly β sheets are less likely to form than a helices during the earliest stages of protein folding. Explainwhy this is the case. (hint: think about the hydrogen bonding requirements)
Nearly all bacteria contain peptidoglycan. Review the structure of peptidoglycan by selecting the correct characteristics listed below. Check All That Apply Polymer of alternating N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) Contains a tetrapeptide that extends from N-acetylglucosamine (NAG) Contains D-amino acids not found in proteins All bacteria use a peptide interbridge to connect the sugar strands Peptidoglycan is a strong and rigid structure
Which amino acid sequence will form part of which protein structure, and why? Sequence 1: Ser-Phe-Gln-Val-Lys-Leu-His-Tyr-Asp-Val Sequence 2: Glu-Tyr-Leu-Asn-Phe-Ala-Gln-Val-Leu-Arg __Amphipathic beta strand __ Amphipathic alpha helix

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Which type of motifs/folds are found in the protein shown below O Colled-coil O EF Hand O Horseshoe O Rossmann O Jelly roll O Greek key O Alpha/beta barrel O Beta barrel O Beta sandwich OZinc finger