Biological Science
5th Edition
ISBN: 9780321743671
Author: Scott Freeman
Publisher: PEARSON
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Chapter 3, Problem 14TYPSS
Summary Introduction
To review:
A concept map relating the four levels of protein structure and showing the formation of hemoglobin including the following terms: primary structure, secondary structure, tertiary structure, quaternary structure, Active site, Amino acid sequence, R-groups, α-Helices.
Introduction:
The different levels of protein structure are referred as primary, secondary, tertiary, and quaternary structure based on the covalent structure and folding patterns. The primary structure of the proteins is made up of the amino acid sequences which are joined together by the help of peptide bonds in a straight line. The secondary structure refers to the basic three-dimensional form of the stretches of the proteins. The tertiary structure consists of the one chain of the polypeptide which acts as the backbone of the structure along with one or many secondary types of protein structures.
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All three types of biopolymers are set from the building blocks with similar types of chemical reactions. Draw the chemical reaction formula for the polymerization reaction. Describe two non-covalent interactions that stabilize a tertiary structure of a protein. c.When describing the structure of proteins, it is often done at different levels. Explain what is meant by the following structural levels: primary structure secondary structure tertiary structure quaternary structure
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- Which way is more common practice to characterize the strength of a binding reaction between a protein and its ligand? Group of answer choices By its binding free energy, delta G By its equilibrium association constant K(A) By its equilibrium dissociation constant K(D) By the rate at which the biding reaction proceedsarrow_forwardWhich 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.arrow_forwardClassify each peptide chain as part of a parallel β sheet, part of an antiparallel β sheet, either type of β sheet, or not part of a β sheet. Parallel β sheet // Antiparallel β sheet // Either // Neitherarrow_forward
- Please don't provide handwritten solution .....arrow_forwardIn 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? ____________________arrow_forwardGive 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 Barrow_forward
- Based upon your knowledge of protein folding, which of the following statements would you expect to be FALSE: O The native state is the protein conformation with the most negative Gibbs free energy value. O The hydrophobic effect causes non-polar side chains to pack into the interior of a protein away from solvent. Proteins are likely to try out every possible conformation before folding into the native state. O A protein incubated in hexane (C6H14) is likely to denature and unfold. O Detergents can interact with the side chains of valine, leucine and phenylalanine.arrow_forwardImagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. Here's what R looks like: -CH- CH HO CH O yes Could R, form a salt bridge with R, at physiological pH, if R₂ were the right kind of residue? O no If you said R, could form a salt bridge with R₂, what would R, have to be? If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the 3-letter code of any of them. Explanation Check Z X E all option H cmd H N J 0 O P cmd optionarrow_forwardWhich of the choices are types of posttranslational modifications a newly synthesized protein may undergo? Select all the choices that apply. changes to hydrogen bonding capabilities formation of an amide bond between Cys and an isoprenyl group removal of prosthetic groups removal of the thiol group from a Cys residue modulation of charges on amino acids proteolytic cleavage covalent attachment of oligosaccharides to Asn, Thr, or Serarrow_forward
- Which of the following is the first step in folding a linear polypeptide into an ordered functional protein? O Secondary Primary Quaternary Tertiaryarrow_forwardAfter denaturation of a tertiary protein like lysozyme (with one polypeptide chain), the only remaining bonds between its monomer subunits will be: the disulfide bonds the van der Waals forces the peptide bonds the hydrogen bonds the ionic bondsarrow_forwardChoose 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 structurearrow_forward
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