Please send me the question in 20 minutes it's very urgent plz Which one is not an example of supersecondary structure?the pyrrole ringthe Greek keythe B-meanderO the B-barrelO none of the choicesProteins that aid in the correct and timely folding of other proteins are calledJaKTelRefer to the structure above. The type of bonding labeled "N" in this figure is:O Hydrogen bonding of the peptide backboneO Covalent bonding involving the R-groupsO Hydrophobic interactionsO Metal ion coordinationElectrostatic attraction

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Which one is not an example of supersecondary structure? the pyrrole ring O the Greek key the ß-meander O the ß-barrel none of the choices Proteins that aid in the correct and timely folding of other proteins are called Le 11011111 P Refer to the structure above, The type of bonding labeled "N" in this figure is: O Hydrogen bonding of the peptide backbone Covalent bonding involving the R-groups O Hydrophobic interactions O Metal ion coordination O Electrostatic attraction

Which one is not an example of supersecondary structure? the pyrrole ring O the Greek key the ß-meander O the ß-barrel none of the choices Proteins that aid in the correct and timely folding of other proteins are called Le 11011111 P Refer to the structure above, The type of bonding labeled "N" in this figure is: O Hydrogen bonding of the peptide backbone Covalent bonding involving the R-groups O Hydrophobic interactions O Metal ion coordination O Electrostatic attraction

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 19QP: Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the...

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Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
Select the properties that apply to the secondary structure alpha helices (select all that apply). U 0 can be Antiparallel can be Parallel are typically right handed are typically left handed obeys n+4 rule are formed by the pattern of hydrogen bonding the backbone makes with itself are formed by the pattern of covalent bonds the backbone makes with itself are formed by the pattern of electrostatic attractions the backbone makes with itself
Which type of motifs/folds are found in the protein shown below Coiled-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
Part B The full structure for the polypeptide found in wasp venom is shown. Identify the individual amino acids in the structure below. Drag the appropriate labels to their respective targets. lle Asn Leu Lys Ala Val Gln Asp Submit HN **** H₂N Request Answer NH₂ TI NH₂ 0= 16 NH₂ Reset Help NH₂
The tertiary structure of a protein is maintained by interactions between the side chains of amino acid residues one such interaction is between cysteine residues, sketch a covalent bond link that can form between side chains of two cysteine residues. Only relevant atoms that can form the link need to be shown
Give the force of interaction involved in the protein folding of the protein structure A and C: COO CH,C-N-H• • •0- Pleated sheet structure A H C Helical structure CH3 CH3 - CH3 -CHCH,CH, CH- CH, CH3 (CH,),NH, -0-CCH,- C=0..•HN CH, CH, CH,CH CH,CH CH, CH, CH OH 0=C -CH,-S,S-CH,- H,Ñ Structure A: H-bonding: Structure C: Van der Waals O Structure A: Covalent interaction; Structure C: dipole-dipole interaction O Structure A: Salt bridge: Structure C: H-bonding Structure A: Hydrophobic interaction; Structure C: ionic interaction 00000 B
Which of the following is the TRUE statement? When found together, a helices and B sheets are generally found in the same structural 'layer The B conformation is most stable when the individual segments are twisted in a left-handed direction Hydrophobic interactions make a large contribution to the stability of protein structures, therefor, burial of hydrophobic amino acid residues need at least two layers of secondary structure The backbone segment of a ß conformation polypeptide segment can readily H-bond to an a helix adjacent to it
Which of the following statements concerning the peptide NH3*-Val-Ala-Gly-Lys-Leu-Gly-Val-Phe- Tyr-lle-COOH is correct? O The peptide can form an alpha-helical secondary structure O The peptide can form a beta-pleated sheet O The last amino acid residue is Val. O Three peptide linkages are present.
The amino acid proline (Choose all that apply) O Is a residue frequently found in secondary structure, turns Has an ionizable side group at pH 7.0 O Has a side chain hydroxyl group O Has a free a-amino group Has a free a-carboxyl group O Has a side chain group sulfhydryl group Is a residue frequently found in secondary structure, a-helix O Has a polar side chain
The different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bonds
A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypep- tide. Fragments are grouped according to size. Pentapeptide Fragments Tetrapeptide Fragments Phe-Val-Asn-Gln-His Gln-His-Leu-Cys His-Leu-Cys-Gly-Ser His-Leu-Val-Glu Gly-Ser-His-Leu-Val Leu-Val-Glu-Ala
Which of the following statement is not true? In a secondary structure the consecutive residues have phi and psi values that are quite different. The Ramachandran diagram defines the restrictions of polypeptide backbone conformation. Two α helices with hydrophobic side chains repeated in a regular pattern can form dimeric structures in water. Greek key motifs occur frequently in antiparallel β structures. Both α helices and β sheets can be amphipathic.