answer : when atoms in the backbone of a protein or peptide form
hydrogen bond
within a single polypeptide or between
amide bond chain a
secondary structure results .the two most common secondary
structure are the
and the
Explanation: there are 4 different level of protein structure
i) primary structure:it refers to the sequence of amino acid present in a polypeptide which are joined together by amide bond (NH-CO)
ii) Secondary structure : Because of presence of OH and amine functional groups there is always a chance of hydrogen bonding so to favour this folding of protein occur and the so obtained is secondary structure
iii)tertiary structure : 3 dimensional folding of the protein due to side chain interaction
iv) quaternary structure:protein consisting of more than one amino acid chain
What happens when a primary structure forms a secondary structure? Match the words in the left...
which of the following is not a way in which amino acid structure in sequence might affect the properties of a protein a) Amino acid side chains form peptide bonds with each other causing the molecule to twist into a secondary structure b) Amino side chains interact with each other causing polypeptides to bend into a tertiary structure c) Hydrogen bonding between every fourth amino acid results in the formation of a coil called an a helix d) Hydrogen bonding...
Which of the following is true of secondary structure in protein folding? Pick ALL that apply. A. It involves hydrogen bonding. B. It involves the side chains. C. It involves hydrophobic interactions. D. It results in alpha helicies with the side chains hidden inside the helix. E. It results in beta-pleated sheets with side chains sticking out of the plain of the sheet. F. It involves the peptide backbone.
please answer
5. Secondary structure (B-sheet): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of a B-sheet. The image on the left is of an anti-parallel sheet, and the right of a parallel sheet. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the amino acid (backbone or side chain) are...
Which of the following statements Explain primary,
secondary, tirtially and quaternary structures of protien
Questions for G2: 1) Would you expect to find valine and leucine on the outside or the inside of the tertiary structure? Why? pts) 2) State whether the following statement describe primary, secondary, tertiary, or quaternary protein (15 pts) structure A. Adjacent chains of polypeptides are held together by hydrogen bonds between the O of the carbonyl group of one chain and the H of an...
please answer
4. Secondary structure (a-helix): The image below is of a polypeptide in secondary (2) structure level of protein folding. Specifically it is of an a-helix. Use the image on the left to answer the questions a-e below. The image on the right is to help with question "f' only. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? c. Is this bond/interaction permanent or transient? d. What parts of the...
Review| Constants| Periodic Table Protein structure is conceptually divided into four levels, from most basic to higher order Primary structure describes the order of amino acids in the peptide chain. Secondary structure describes the basic three-dimensional structures, a-helices and B sheets. Tertiary structure describes how the secondary structures come together to form an individual globular protein. Quatemary structure results from individual proteins coming together to form multi-subunit protein complexes Part A Complete the following vocabulary exercise relating to the level...
The type of bonding that maintains the secondary structure in a protein is theA) Hydrogen bonds between the carbonyl and amino groups of the backboneB) Covalent bond between the carbonyl and amino groups of the amino acidsC) Hydrogen bonds between two amino acidsD) Disulfide bonds that hold two polypeptide chains togetherE) Hydrogen bonds between two amino groups
pls
answer 6 and 7
6. Secondary structure (turn): The image below is of a polypeptide in secondary (20) structure level of protein folding. Specifically it is of a turn. Turns vary in length. The shorter the turn the more drastic the angle changes. The longer the turn, the more gradual the angles needed. a. Name the specific bond/interaction indicated by the dotted lines. b. Is this bond/interaction covalent or non-covalent? Is this bond/interaction permanent or transient? d. What parts...
added part a of the question for clarity
1. Polypeptides are the natural polymer of the naturally occurring amino acids. Their structure can be considered at various levels to consist of Primary: amino acid sequence secondary: regions of ordered structure (a-helix, B-sheet, etc.) tertiary: overall 3D shape; folding quarterniary: interaction of protein sub-units (a) Consider the following segment of a polyamide H Show the resonance structures for the amide bond (in the box) (i) (ii) Indicate what o and w...
(2%) Indicate which secondary structure or structures (α -helix,
β -pleated, random coil) will the following peptide adopt in an
aqueous solution at pH 7
(2%) The unfolding of the alpha helix of a polypeptide to a
randomly coiled conformation is accompanied by a large decrease in
a property called specific rotation, a measure of
a solution’s capacity to rotate circularly polarized light.
Polyglutamate, a polypeptide made up of only L-Glu residues, has
the alpha helical
conformation at pH 3....