"VDAATFKQANDNG" is the sequence of an a helix. Which of the following interactions is probable? (. denotes a H-bond) N...A F...V V...A Q...A
Q: 3b) Both a-helical 2° structure and b-pleated sheet 2° structure result from the same type of…
A: Proteins are the unbranched polymer of amino acids. They have four different level of structural…
Q: Even peptides with large nonpolar regions may contain alpha helices stabilized by hydrogen bonding…
A: polypeptides form either alpha helical structure or beta sheets stabilized by hydrogen bond.
Q: Which of the following amino acid changes can result from a single base-pair substitution? Explain…
A: Mutations are alterations in the DNA sequence of an organism. Small changes, such as adding or…
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A: Amino acids are the monomers that are bonded by peptide bonds to make polypeptide chains.
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A: Nucleic acids such as DNA and RNA, contain genetic information and information about protein…
Q: What do you mean by double helix ? Explain with the help of a diagram.
A: DNA is the genetic material in most living organisms. It is the information hub of the cell that…
Q: Long-range interactions between residues on a single polypeptide chain are classified as quaternary…
A: Proteins are the linear chain of amino acids attached together via peptide bonds. Proteins are…
Q: 1. a. What is the role of these bond of the polypeptide in determining the secondary structure of…
A: Protein is made up of polypeptides. Polypeptides are the polymer of amino acids and these amino…
Q: Draw the structure of the dipeptide Thr-Cys at pH7. Clearly indicate the following: the amino…
A: A dipeptide is formed between two amino acid residues in which an amino group of one amino acid is…
Q: . Vwhat do you think holds together the various secondary structural elements in a Stickular…
A: These questions are about interactions in amino acids.
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A: Secondary structure of protein describes the special arrangement of its main chain atoms, without…
Q: A particular DNA sequence encodes for MRNA that then encodes for the amino acid glutamate in a…
A: In translation, the newly formed mRNA is decoded in a ribosome. The ribosomes facilitate decoding by…
Q: Within a protein, certain amino acids are positively charged (e.g.,lysine and arginine), some are…
A: DNA or the deoxyribonucleic is the defined genetic material and it is made up of a base, deoxyribose…
Q: A comparison of the aligned amino acid sequences of two proteins each consisting of 150 amino acids…
A: In the given case both the proteins can be of related population so, the proteins can be related by…
Q: β-mercaptoethanol ____, and urea _____ disrupt the interactions involved in formation of α-helices.…
A: DNA stands for deoxyribonucleic acid. It is the genetic material of the organisms that transfer from…
Q: You have discovered a new protein, one whosesequence has about 25% homology with ribonuclease A. How…
A: It is given that a new protein is discovered; whose sequence has about 25% homology with the…
Q: In the amino acid sequence below, the amino acid residue in red was shown to be essential to the…
A: Peptides or proteins are composed of twenty standard amino acids. These standard amino acids differ…
Q: What is the most consistently (i.e. found in every case) energetically unfavorable aspect of protein…
A: People have developed molecular dynamics simulations of the basic atomic forces that determine a…
Q: Some point mutations cause a change in amino acid sequence but nonetheless may have little to no…
A: option f is correct . This is because each group of amino acid belong to same category means . If…
Q: if two polypeptide chains are interacting as alpha helices with the following amino profiles: A:…
A: if two polypeptide chains are interacting as alpha helices with the following amino profiles: A:…
Q: What kind of weak bonds hold the two strands together? How is that weak bond drawn?
A: Answer - Hydrogen bonds (-H) is a weak bond that holds two strands together. Explanation - Each…
Q: What are the Characteristics Binding Site?
A: Binding sites are present in all the macromolecules such as proteins. This binding is done with…
Q: Helices can be described by the notation nm,where n is the number of residues per helical turn and m…
A: Proteins are a type of macromolecule that have a variety of roles in biological processes. It is…
Q: What could be the implications if there is a misfolding in the protein structure?
A: Protein folding is a physical process. In this process, the native polypeptide chain folds into an…
Q: VDAATFKQANDNG” is the sequence of an α helix. Which of the following interactions is probable? (...…
A: The alpha helix structure is a secondary structure found in folded proteins. The alpha helix in…
Q: f an Arg residue in a protein was replaced with either Lys or Glu amino acid, which substitution…
A: Proteins are large biomolecules that compose structural and motor elements of a cell, and also as…
Q: Explain the single-polypeptide chain folds ?
A: Proteins contains one or a lot of molecules of polypeptides. Proteins square measure necessary as…
Q: What is the primary reason the a-helix conformation in polypeptides such a stable form? A. The…
A: The secondary structure of protein determines the local spatial arrangement of the amino acids in…
Q: How do covalent bonds differ from hydrogen bonds? Define base complementarity (refer to…
A: The stable attraction between atom, molecules or ions are called chemical bonds. Molecules and…
Q: In what naturally occurring nucleic acids would you expectto find A-form helices, B-form helices,…
A: Nucleic acid is the genomic component of every cell, which possess entire information of the cell…
Q: why do you think this is? In your explanation, you should describe the specific molecular…
A: 1. Proline is rarely found in beta sheets or alpha helices this is because proline is totally…
Q: Which of the following peptides is most likely to form an a-helix? ETAEKAFKQYANDN GLLKQSTQCLEVKT…
A: Most of the alpha-helix are transmembrane proteins
Q: 57. Renaturation may be expected in the denatured proteins of which of the following cases? A.…
A: In molecular biology, renaturation refers to the restoration of a protein or nucleic acid (such as…
Q: Consider the following amino acid sequence :a)Where might bends or βturns occur? b)Where might…
A: Polypeptides are polymers of amino acids, in which consecutive amino acids are linked by peptide…
Q: c. Label each amino acid as polar, non-polar, or electrically charged d. Label the N-terminus and…
A: Introduction Amino acids are the building blocks that adjoin together by a peptide bond to form a…
Q: List some of the possible combinations of α-helices and βsheets in supersecondary structures.
A: The helix and the pleated sheet are the two most important secondary structures. Hydrogen bonds…
Q: transmembrane portion of an alpha helix?
A: The alpha-helix is a coiled structure made up of proteins which consists of single chain of amino…
Q: A protein has a clearly defined hydrophobic core; however there is the residue glutamine within the…
A: The correct option is (a) Hydrophobic interactions
Q: Can a mutation change a protein’s tertiary structure without changing its primary structure? Explain…
A: Every function in living beings depends on proteins. There are different types of proteins and each…
Q: Draw the structure of STVWY at pH 13. Connect with an arrow the C=O of the N- terminal residue to…
A: The given peptide is composed of five residues. The name of the fiver residues from N-terminal to…
Q: 3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of…
A: Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will…
Q: Suppose that a polypeptide contained one aspartate (Asp) residue and one arginine (Arg) residue and…
A: Biomolecules are organic molecules made up of mainly carbon and hydrogen, but other elements are…
Q: Which of these peptides is the most hydrophobic? A. KFYV B. ERSC C. PIMF
A: Proteins are modified polypeptide chains. These chains are made up of 10 or more amino acids linked…
Q: Which of the following peptides will likely adopt an alpha helix? H-I-R-E-F A-D-L-E-E A-D-E-L-E…
A: The most common types of secondary structure are alpha-helix and beta-pleated sheets. The…
Q: Two peptides have almost the exact same primary structure, except that one has about 10 fewer amino…
A: Proteins or peptides have significant roles in our bodies. They are the building blocks of the body.…
Q: If a quaternary (4°) protein structure has six N-terminus. How many total subunits does it have?
A: Proteins are the most important macromolrcules in the body. The proteins has definitely structural…
Q: 2. Of the two sequences, which is more likely to have helical structure. Explain. a)…
A: The amino acids are the protein structure alphabet; they can be arranged to create an almost…
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- Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys CysD raw the full structure of the following tetrapeptide . Label the N terminaland C terminal residues. Phe - Cys - Ser - IleBIOCHEMISTRY If the protein is more hydrophobic, then adding additional charge is not the best strategy. What are other excipients we might select instead of NaCl to try to interrupt these interactions?
- Within a protein, certain amino acids are positively charged (e.g.,lysine and arginine), some are negatively charged (e.g., glutamateand aspartate), some are polar but uncharged, and some are nonpolar.If you knew that a DNA-binding protein was recognizingthe DNA backbone rather than a base sequence, which aminoacids in the protein would be good candidates for interacting withthe DNA?INSTRUCTIONS — Answer the Question properly and accordingly — Do not copy in Google, or here in Bartleby QUESTION • Name the four different types of interactions responsible for creating tertiary structures in proteinsIt is observed that as temperature is increased, most protein molecules gofrom their defined, folded state into a random-coil, denatured state thatexposes more hydrophobic surface area than is exposed in the folded state.(a) Given what you have learned so far about ΔH and ΔS, explain why thisis reasonable. (b) Sometimes, however, proteins denature as temperature is decreased.How might this be explained?
- Most proteins require molecular chaperones toassist in their correct folding. How do you suppose thechaperones themselves manage to fold correctly?Chemistry Consider a protein with a beta conformation sequence EAGQVHRGP a) Which residue(s) can be substituted by N without affecting the conformation? b) Which residue(s) can be substituted by D without affecting the conformation? c) Which residue(s) cannot be substituted without affecting the conformation?Draw the structure of 2 five-mers (draw backbones with side chains shown as R groups) forming a beta sheetwith two anti-parallel beta strands. Indicate the hydrogen bonds present inthissecondary structure.
- Proteins that are synthesized by living organisms adopt abiologically active conformation. Yet when such moleculesare prepared in the laboratory, they usually fail to spontaneously adopt their active conformations. Can you suggestwhy?Need help. Which one of the following statements is FALSE? Group of answer choices A.Beta-pleated sheets are part of the secondary structure of proteins B.The nitrogenous bases of DNA are located on the inside because they are hydrophobic in character C.The peptide bond is formed by dehydration synthesis D.Alpha helices are stabilized by attraction between the amino acid R groups E.The peptide bond is rigid and planar and has partial double bond characterParallel beta sheets are less stable than antiparallel beta sheets, becasue they have __________ hyrdogen bond. Fill in the blank less or more?