Both please Which protein structural features are apparent in the protein structure below?Select all that applyQuaternary structureParallel beta sheetAntiparallel beta sheetAlpha-helixCoenzyme Which of the following is an enthalpically favorable contribution to the stability ofprotein structure?Select all that apply.Hydrogen bondsdipole-dipole interactionsLondon's forcesion-dipole interactionsHydrophobic effectDisulfide bonds

Different bonds contribute to protein folding. These bonds are hydrogen bonds, hydrophobic bonds,…

Answered: Which protein structural features 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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After carefully reviewing the material (CS links, slides, etc) complete the table about various bonds present in all four levels on proteins' conformation. You need to make a 4x4 table (see below how to make one) to put + and - signs for Yes or No. Bond types Primary Secondary Tertiary (Quaternary) Task: no response to others is needed; just post before your class. Searchentries hon Unread 12t Parrah BIVA Ev Tv v v め▼ レm 2 E Te Tale ppertie K Delete Cel Row Calum Su Search entries or author Unread 2/2 6 Reply sert delete home end prt se Tum backspace tock %23 5 T Y E enter F H K D shift C V B N pg dn pg up alt ctrl Spaced Reption. Day one- Da82 Protein levels Covalent puoq-H lonic Van der Waals
Which of these statements about the tertiary structure of a polypeptide is(are) untrue? You may select more than one answer. The tertiary structure will be maintained when the solvent is changed from pure water to aqueous acetic acid. O The tertiary structure is determined in part by the formation of disulfide bridges. Hydrogen bonding interactions are responsible for formation of secondary structure but not tertiary structure, O The tertiary structure is rigid and unchanging. O Charge-charge (electrostatic) interactions can be important in the tertiary structure.
The dihedral or torsion angles of polypeptide backbone, the allowed values of which are summarized by the Ramachandran diagram, refer to rotation of the following pair of bonds. Cα-N and Cα-R C=O and Cα-N C-N and Cα-C Cα-C and Cα-N Cα-R and Cα-C
Shown below is the structure of a polypeptide with the pK, values of its acidic hydrogens. pK = = 10.1 H OH pK, = 9.2 H. pKa = 2.1 H. N-H pK, = 6.0 pKa = 3.9 1. How many peptide bonds are present in one molecule of the polypeptide? [ Select ] II. Over what pH range would this molecule predominantly exist in a state that has a net charge of zero? [ Select ] ZI
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
Choose the best response for each of the blanks in the statement below. When it is part of a polypeptide chain, proline is a known disruptor of [Select] because of [Select] [ Select ] its hydrophobic character the strain brought about by the five-membered ring the lack of an amino hydrogen in the backbone the lack of a freely moving side chain Select ] primary structure secondary structure tertiary structure quaternary structure
What types of interactions are possible between the side chains of the polypeptide shown below? Select all that apply: *NH, он SH SH H H N, N, N, H H H NH2 *NH, O Disulfide bonds O Hydrogen bonds lonic bonds O Hydrophobic interactions
Label the N- & C termini Label ALL alpha -carbons (with an alpha) Label ALL peptide bonds(highlight or draw an X through these) Circle all AAresidues label which ones are nonpolar, polar,-acidic, & basic For each side chain, label/identifywhat types of R - group interactions it canparticipate in (H - bond, disulfide bond, ionic/electrostatic interactions, or hydrophobicinteractions.) Peptide Structure
Part A What is the highest structural level of protein structure represented in the following image? primary quaternary secondary pentanary tertiary O O
the resonance stabilization of the amide linkage has profound effects on protein structure. Which of the following are the direct effect(s) of this on protein structure? Select all that apply All six atoms around the bond (including the Co) lie on the same plane There is no free rotation about the peptide bond. The bond between the carbon and the nitrogen in the peptide bond keeps "flickering" between being a single bond and a double bond. The peptide bond is polar. The nitrogen in the peptide bond cannot accept a hydrogen bond.
Electrophoresis is the movement of molecules within a matrix (paper, gel) to which an electric field is applied – from a central origin, a molecule with a net positive charge moves toward the negative pole (often called cathode) and a molecule with a net negative charge moves toward the positive pole (often called anode). for the pentapeptide: N – Lys - gly - asp - his - glu - C What is the net charge at pH 3? 2.What is the net charge at pH 11? 3. At pH 3 will the pentapeptide move to the negative pole, positive pole or not move? 4. At pH 11, the same question.
draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 and put each charges beside the amino acids then compute for the isoelectric point please show complete solution KRINPLA

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Which protein structural features are apparent in the protein structure below? Select all that apply Quaternary structure Parallel beta sheet Antiparallel beta sheet Alpha-helix Coenzyme