In the alpha helix shown below, all carbonyl groups are pointing_amino groups are pointing.Downwards; DownwardsDownwards; UpwardsUpwards; DownwardsUpwards; Upwardsand

The secondary structure of a protein refers to the folded configuration of the polypeptide chain.…

Answered: In the alpha helix shown below, all…

Biology Today and Tomorrow without Physiology (MindTap Course List)

5th Edition

ISBN:9781305117396

Author:Cecie Starr, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Christine Evers, Lisa Starr

Chapter7: Gene Expression And Control

Section: Chapter Questions

Problem 2CT

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In hinge region, what is the most prominent amino acid existing? A B C D E proline G F
A helical wheel is a two-dimensional representation of a helix, a view along its central axis. Label the blanks on the helical wheel diagram to show the distribution of amino acid residues in a helical segment with the sequence -Val-Asp-Arg-Val-Phe-Ser-Asn-Val-Cys-Thr-His-Leu-Lys–Thr-Leu-Gln-Asp-Lys- 1 Answer Bank H L D K R F T K S T
Which amino acids would you expect to find marked on the alpha helix? Alanine Isoleucine Leucine Methionine Phenylalanine Tryptophan Valine 000000 |||| |||||| ||||||||| 000000 Nonpolar side chains; hydrophobic Side chain (R group) H₂N H₂N C 0 H₂N HO Glycine (Gly or G) CH₂ H₂N CH₂ CH₂ OH CH₂ CH₂ Methionine (Met or M) Polar side chains; hydrophilic HO Alanine (Ala or A) CH₂ H.Nº C C-O HO Phenylalanine (Phe or F) ỖI 0-0 SH он сн CH₂ CH OH₂NCCO H₂N*CCO Acidic (negatively charged) 0 0 Serine Threonine Cysteine (Ser or S) (Thr or T) (Cys or C) Electrically charged side chains; hydrophilic CH₂ CH₂ CH₂ CH₂ CH H₂NCCO H₂NCCO H₂NCC o HO Aspartic acid Glutamic acid (Asp or D) (Glu or E) HO Valine (Val or V) 000000000 ||||| ||||| ||||||| 00000000 NH₂ OH H₂N HẲN Ô CÓ HO Tryptophan (Trp or W) CH₂ H₂N² сCO 0 CH₂ CH₂ H₂NCCO HO Lysine (Lys or K) 0 Leucine (Leu or L) NH CH₂ CH₂ CH CH₂ NH₂ H₂N® CH₂ Tyrosine (Tyr or Y) Asparagine (Asn or N) Basic (positively charged) NH₂ CNH, NH CH₂ CH₂ CH₂ H₂NCCO HO…
To visualize the spatial arrangement of amino acid residues in an a-helix, it is helpful to imagine you are looking down the long axis of the helix, just as you would look down a soda straw. Viewed in this orientation, the residues form a circle, with each residue offset from its neighbor by 100 degrees. This representation is called a helical wheel. Use the circle below to indicate the position of each residue around the helix of the enzyme lysozyme. NH ...Arg - Cys - Glu- Leu - Ala Ala - Ala Met-Lys COO- The first two amino acids, Arg-1 and Cys-2, are shown as an example. Arg-1 O Glu-3 Which amino acid in the polypeptide is the first to pass the origin (i.e., which amino acid passes Arg- 1 first, completing one full circle)? Select the best answer. O Leu-4 O Ala-5 O Ala-6 O Ala-7 Met-8 O Lys-9 100° O none of the above Cys-2
In the following polypeptide, which amino acid would be participating in hydrogen bonding with alanine, given this sequence forms an alpha helix? Please write out the full amino acid name, not the abbreviation. Met-Ala-Leu-Glu-Lys-Thr-Leu-Val
One common secondary structure found in proteins in the a-helix. On the diagram below is an a- helical region of the enzyme lysozyme. The sequence of this region is: NH Arg - Cys - Glu - Leu - Ala-Ala-Ala-Met-Lys. COO- 0 0 on the top 0 on the bottom R Is the N-terminus on the top or on the bottom of this diagram? R
I-D-E-L-Y-S-Q-V-C-S-H-L-D-T-V-R This amino acid sequence forms an alpha helix. When thinking about how the helix folds into its tertiary strucutre, use entropy and enthalpy to explain what would happen energetically.
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
In class we learned about the H-bonding pattern in an alpha-helix. Asp 61 of the spidroin CTD has a slightly unusual H-bonding feature within the helix. That is because it forms three H-bonds. They are H-bonds between its carbonyl oxygen and , between its amide hydrogen and , and between its side chain and Hint: by clicking once on the ribbon diagram at any spot, the model will show H-bonding in that spot.
The structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond towards the C-terminal end of the helix while the hydrogens of the NH groups orient toward the N-terminal end, thus imparting a dipole along the length of the helix. As a result, which kinds of amino acids would favor the C-terminal end, and which would favor the N-terminal end? negatively charged, positively charged positively charged, negatively charged negatively charged, hydrophobic positively charged, hydrophobic hydrophobic, negatively charged hydrophobic, positively charged
Glycosylation is a major type of protein post-translational modification. Identify the amino acid that is joined to each monosaccharide by a glycosidic bond. glycoprotein A glycoprotein B glycoprotein C HA HO Н CH₂OH HO OH Н H CH₂OH Н ОН HO HN-C-CH3 о c=0 NHI -NH-C - CH2C-H ОН Н нн ОН НН CH2OH Он OH HO Н NH 1 С=0 -CH2-C-н NH C=0 LO-CH2-C-H NH A В с
Which statement is true regarding an a helix, there are five residues per helical turn. the helix is right-handed there are usually many proline residues present. side chain residues point up and down the axis of the helix.

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