ch one of the following statements about protein structure is NOT correct? . Domains are discrete parts of a protein structure, usually associated with a particul function. true Beta-sheets are stabilised by hydrogen bonds between amino-hydrogens and carbonyl-oxygens from peptide bonds. no adjacent hydrogen bonding Proteins made from three polypeptide chains show quaternary structure. Yes Smaller protein domains come together to from supersecondary structures and m-

ch one of the following statements about protein structure is NOT correct? . Domains are discrete parts of a protein structure, usually associated with a particul function. true Beta-sheets are stabilised by hydrogen bonds between amino-hydrogens and carbonyl-oxygens from peptide bonds. no adjacent hydrogen bonding Proteins made from three polypeptide chains show quaternary structure. Yes Smaller protein domains come together to from supersecondary structures and m-

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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Match the following levels of protein structure with their description two or more polypeptide chains > > twisting and folding to form a 3-dimensional structure, dependent on the locations of the charged groups and polar groups within the amino acid chain, sometimes covalent bonds form between sulfur atoms (called disulfide bonds) alpha helix and beta- pleated sheets formed by the arrangement of hydrogen bonds between amino acids, many other shapes are possible amino acid sequence 1. quaternary 2. tertiary 3. primary 4. secondary
Protein structure is directly related to function. Which of the following statements is true regarding this concept ? Polypeptide backbone -CH2 – CH, – CH2- CH2- NH3 0-c- CH - CH2 lonic bond Hydrogen ! bond C- NH2 Disulfide linkage CH CH2 HạC CH3 CH3 H3C CH -CH2 Hydrophobic interactions A. The primary structure consists of the DNA sequence. The secondary and tertiary structures are dependent on interactions between the DNA and RNA polymerase. Mutations resulting in changes one or more bases has the potential to destroy the structure, and therefore the function, of the protein. B. The primary structure consists of the amino acid sequence. The secondary and tertiary structures are dependent on interactions between the amino acid side chains. Mutations resulting in changes one or more amino acids has the potential to destroy the structure, and therefore the function, of the protein. C. The primary structure consists of the DNA sequence. The secondary structure consists of the amino acid…
Part A What is the highest structural level of protein structure represented in the following image? primary quaternary secondary pentanary tertiary O O
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
Match the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)
A protein has higher order structure. Which statement about higher order structure of proteins is true? Group of answer choices A protein's primary structure is its amino acid sequence. The quaternary structure of a protein is comprised of its alpha helices and beta pleated sheets. Polypeptide subunits combine to form a protein's tertiary structure. All previous answers None of these answers
Which one of the following statements about the structure of proteins is incorrect? O Disulfide bonds provide strong intrachain interactions. Hydrogen bonding stabilizes the a-helix proteins. Nonpolar groups tend to face the outside of a protein in an aqueous solution. lonized amino acid side chains can form salt bridges within a protein. O Heat can disrupt tertiary structure.
Hydrogen bonds that form a helices and B-pleated sheets are the primary interaction in which level of protein structure? O secondary O quaternary O primary O tertiary
Select the true statements about protein secondary structure. In an a-helix, the side chains are located on the outside of the helix. The secondary level of protein structure refers to the spatial arrangements of short segments of the protein. In a B-pleated sheet, the side chains are located between adjacent segments. Peptide bonds stabilize secondary structure. The x-helix is held together by hydrogen bonds between the amide N-H and C=O groups. Incorrect
For this homework it’s a protein but I am stuck because it asks This molecule can have _____ levels of structure And then it asks What level of structure is shown in this protein marcromolecule Then asks if I add another chain to this molecule what level of structure will that be? What are the other levels of structure it can have and how are they formed
In the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing?
Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data Consider the following amino acid sequence Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg Where might reverse turns occur? Where might Intrachain disulfide linkages be formed? What will be the secondary structure formed from this sequence? Assuming that this sequence is part of a larger globular protein, indicate the probable location of the following amino acid residues: Asp, Ile, Thr, Ala. Gln, Lys.( Hint: see Hydropathy index)