The tertiary structure of a protein is maintained by interactions between the side chains of amino acid residues one such interaction is between cysteine residues, sketch a covalent bond link that can form between side chains of two cysteine residues. Only relevant atoms that can form the link need to be shown

The tertiary structure of a protein is maintained by interactions between the side chains of amino acid residues one such interaction is between cysteine residues, sketch a covalent bond link that can form between side chains of two cysteine residues. Only relevant atoms that can form the link need to be shown

Nutrition Now

8th Edition

ISBN:9781337415408

Author:Brown

Publisher:Brown

Chapter15: Proteins And Amino Acids

Section: Chapter Questions

Problem 12RQ

See similar textbooks

Similar questions

Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
Which 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.
Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. In the table below are four possibilities for what R, and R, might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ threonine cysteine glutamine arginine cysteine tyrosine phenylalanine glutamate specific interaction? Oyes no yes O no O yes O no Oyes O no name of specific interaction 0 0 0 0 X
The different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bonds
Which of the following most directly applies to the formation of the secondary structures of proteins? A B с D formation of ionic bonds between the R groups of two polypeptides formation of nonpolar interactions between two R groups on the same polypeptide formation of covalent bonds via dehydration reactions between two amino acids formation of hydrogen bonds between between amino and carboxyl groups
Draw the protein folding pattern when the polypeptide is immersed in water and in oil. Justify your answers by using chemical explanations. In the structure, point all possible types of intramolecular forces of attraction possible for this polypeptide in the indicated solvent system and discuss each. Discuss your answer H3N*-ala-ile-trp-arg-gly-ala-his-tyr-trp-gly-gly-tyr-arg-ile-val-thr-ile-trp-cys- met-gly-ile-asp-cys-thr-glu-cys-trp-gly-cys-phe-arg-his-pro-val-phe-CO-
Which of the following statements best describes the hydrophobic character of bacteriorhodopsin (2BRD)? Both the interior and exterior of the protein are hydrophobic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, but the central core of the trimer is hydrophobic. Both the interior and exterior of the protein are hydrophobic, but the central core of the trimer is hydrophilic.
The simplest form of the Ramachandran diagram is calculated by ignoring hydrogen bonding, interactions with water, and the hydrophobic effect. Why is this simple form of the diagram still an effective predictor of protein backbone conformation?
Identify which amino acid pairs below will not form R-group interactions necessary for the tertiary structure of a protein. threonine and valine glutamine and asparagine phenylalanine and arginine serine and tyrosine
Draw the chemical structure of an alanine pentapeptide. Indicate the location of each peptide bond. Label the phi () and psi () dihedral angles. Name and briefly define the four levels of protein structure.
At what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.