Please provide explanations and work for each part of the question. If able to keep the same format of the question - the table with the answers within along with explanations - that would be the best case. This is biochemistry. Thank you A major difference between protein and DNA is that DNA has the same double-stranded structureno matter what the content or order of the nitrogenous bases, but proteins have a different shapedepending on the content and order of the amino acids. Evolution has led to proteins that fold intoprecise shapes, whether globular, tubular, fibrous, spherical, or netlike, based on how the polypep-tide chain folds. It folds a bit at a time, making and breaking molecular interactions as it folds.To describe these shapes, the four levels of protein structure were named primary, secondary,tertiary, and quaternary.The interactions formed in a protein as it is synthesized and then as it folds are the peptidebond, the hydrogen bond, ionic bonds, polar interactions, disulfide bonds, and hydrophobicinteractions.In the following chart, match each level to the interaction types that form it and to theprotein motifs or features generally ascribed to it. The possible interaction types and motifs tochoose from are listed in the boxes following the chart.LEVELPrimarySecondaryTertiaryQuaternaryInteraction Types■ Disulfide bondHydrogen bondHydrophobic interaction▪ lonic bondPeptide bondPolar interactionINTERACTION TYPEMOTIF/FEATURE ASCRIBED TO THAT LEVELMotif/Features Ascribed. a-helix. B-sheet▪ B-turn. Barrel. Fold▪ Hexameric structure. Overall 3D shape■ Polypeptide chain. Protein domain• Tetrameric enzyme

Protein structure is a fundamental concept within biochemistry, encompassing the hierarchical…

Please provide explanations and work for each part of the question. If able to keep the same format of the question - the table with the answers within along with explanations - that would be the best case. This is biochemistry. Thank you

Please provide explanations and work for each part of the question. If able to keep the same format of the question - the table with the answers within along with explanations - that would be the best case. This is biochemistry. Thank you

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Related questions

Q: Classify the fold of each domain as all a (or mostly a), all b (or mostly b), a/b, or a+b.. 1.…

A: 1.Firmicute collagen-binding protein (1FCB):Fold: All beta (mostly b)Domain classification: all…

Q: The process by which messenger RNA codes for the synthesis of a specific protein is called: a)…

A: The central dogma of molecular biology is a theory that states that the genetic information encoded…

Q: Draw a diagram of a Ramachandran plot. Indicate the location on the plot of an amino acid residue…

A: There are four types of biological macromolecules- proteins, nucleic acids, lipids and…

Q: Label the key components of a matrix-assisted laser desorption/ionization time-of-flight, or…

A: Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALD1-TOF) is a…

Q: The equilibrium constant of a system, K, can be related to the standard free energy change, AG,…

A: Details

Q: Enzymes are important molecules in biochemistry that catalyze reactions. The energy diagram…

A: There are four types of biological macromolecule: proteins, nucleic acids, lipids and…

Q: You are working at a major pharmaceutical company, and you have purified an engineered enzyme, and…

A: To determine the protein stability (ΔG in kJ/mol) using the provided equilibrium unfolding data, you…

Q: The major secondary structure seen in collagen is: a) alpha helix b) beta sheet c) collagen…

A: We provide the answer to the first question. Please repost your question separately for remaining…

Q: You have isolated a protein from the bacterium E. coli and seek to confirm its identity by trypsin…

A: Mass spectrometry is an analytical gel-free proteomics method used for identification of proteins,…

Q: Which of the following amino acids are more likely to be on the interior of the protein? And which…

A: Amino acids are classified as hydrophobic, hydrophilic and neutral based on the property of the side…

Q: For the reaction 2NH3(g) 3H₂(g) + N₂(g) the equilibrium concentrations were found to be [NH3] =…

A: The equilibrium constant of a chemical reaction is the ratio of the product of the active masses of…

Q: 8. Which of the following fatty acids is most likely to be a liquid at room temperature? ОН -H OH OH…

A: Fatty acids are carboxylic acids with a hydrocarbon chain ranging from 4 to 36 carbons. In fatty…

Q: For a reaction to be spontaneous, which of the following factors should have a negative sign? OA…

A: For any reaction to be spontaneous, the change in Gibb's free energy, must be negative (i.e less…

Q: Consider a protein in which a negatively charged glutamic acid side chain (pKa = 4.2) makes a salt…

A: Salt bridges are attractive interactions between two oppositely charged groups. So, more oppositely…

Q: In each case, these are enzymes that catalyze thesame reaction in different species. The question…

A: 1.Aminopeptidases (PR1A from mammal and PR1B from malaria parasite):First, obtain the…

Q: Streptavidin AP washing buffers purpose?

A: Streptavidin Alkaline Phosphatase (AP) washing buffers are essential for molecular biology and…

Q: Classify each peptide chain as part of a parallel β sheet, part of an antiparallel β sheet, either…

A: Beta-sheets are one of the most common secondary structures seen within proteins. Several…

Q: If, in addition to the constraints on glucose concentration listed previously, we have in the liver…

A: To determine the theoretical concentration of glucose-6-phosphate at equilibrium in a liver cell…

Q: What are the molecular weights of the protein X polypeptides? (pick 1 only) - 50 kDa each - 60 kDa…

A: Native PAGE is a technique that uses non-denaturing gels (in the absence of SDS or any denaturing…

Q: Calculate the equilibrium fraction of GAP from the above, at 37 ∘C?

A: The standard change in free energy is related to equilibrium constant by the equation Keq=…

Q: 1. In a catabolic pathway, metabolite X gets converted into metabolite Y, metabolite X metabolite…

A: is the standard change in Gibbs free energy i.e. the change in Gibbs free energy under standard…

Q: 4. What is the conjugate acid of each of the following bases? (do not include a counterion) (a) H₁…

A: A pair of substances which differ by a proton (H+) ion is a called conjugate-acid base pair.The…

Q: Match each error with its consequence for protein purification by column chromatography. Incorrect…

A: Column chromatography is a separation technique that uses a stationary phase and a mobile phase to…

Q: 7. A protein has a molecular mass of 400 kDa when measured by gel filtration. When subjected to gel…

A: As we know that the sodium dodecyl (SDS) sulfate is considered as the denaturing agent, which helps…

Q: Which of the following define the stereochemistry of alanine (as per the structure shown)? Note:…

A: stereochemistry can be defined as the arrangement of functional groups on the alpha carbon atom with…

Q: Which of the following statements is not true about triacylglycerols? When hydrolyzed, they produce…

A: Triacylglycerols, often referred to as triglycerides, are a class of lipids that serve as a primary…

Q: Suppose Gina climbs a high mountain where the oxygen partial pressure in the air decreases to 70…

A: Consider the following reaction: where P is the protein, L is the ligand, PL is the protein-ligand…

Q: What protein has the code 6JX7 in the protein data bank? protein A. membrane B. spike protein C.…

A: The Protein Data Bank (commonly referred to as PDB) is an open access database containing…

Q: QUESTION : Enzymes can be regulated in a many different ways. Covalent modification is one way.…

A: Enzymes are protein-based biomolecules. They speed up chemical reactions. They take part in a…

Q: Which of the following molecules is richest in energy when metabolized? Glucose Linolenate, a fatty…

A: Glucose is the primary source of energy for the body. When there is no glucose available, the body…

Q: What is the IUPAC name for the following molecule? Sc

A: IUPAC nomenclature rules for alkanes:• Identify the longest continuous carbon chain.• Identify the…

Q: Eukaryotic cells contain many compartmentalized organelles. Label the organelles in this eukaryotic…

Q: Select the choice that best describes the stereochemistry of the following amino acid, and rank the…

A: Cysteine is one of the 20 standard amino acids that serve as the building blocks of proteins. It is…

Q: Consider the following peptide: Lys-His-Asp-Glu-Phe-Cys-Ala-Asp-His-Arg What is the net charge of…

A: Amino acids are amphoteric. At a given pH, state of ionization of alpha-carboxylic acid group (pK1),…

Q: 2 a- b- Nucleic acid chemistry Why does lowering the ionic strength of a solution (decrease the salt…

A: DNA is the nucleic acid that acts as the genetic material of life forms. It is a primarily a polymer…

Q: 1.How to prepared SC Yeast Media Buffered with HEPES pH 6.75?

A: In yeast cell culture research, SC (Synthetic Complete) Yeast Media buffered with HEPES at pH 6.75…

Q: Draw a diagram of the aspartic acid side chain in the protonated and unprotonated states. Calculate…

A: The four classes of biological macromolecules are proteins, nucleic acid, lipids and…

Q: Which of these amino acids is a polar, uncharged amino acid? (Select all that apply, if necessary.)…

A: Amino acids are defined as the organic compounds that have amino (-NH3) and carboxylate (-COO- )…

Q: Suppose the concentration of glucose inside a cell is 0.5 mM and the cell is suspended in a glucose…

A: Details

Q: Which one statement below is true about the metabolism of rizatriptan? N N-N ZI rizatriptan MaxaltⓇ…

A: 3.It is a prodrug that is activated by esterases.Rizatriptan is indeed a prodrug, which means it is…

Q: If a pure solution of sphingomyelin was placed in water, would the sphingomyelin molecules interact…

A: The four classes of biological macromolecules are proteins, nucleic acid, carbohydrates and…

Q: Discussing the Data - Class Average vs Group 9. Use the % change my group for the unknown a. Square…

A: The following worksheet contains so many questions and many of them are solved. Those unsolved are…

Q: Determine how many domains and list the residues in each domains (ei. 1-230, 1-120) Vertebrate Ca…

A: The following table explains the answer.Protein-4 VCA( vertebrate Ca 2+ dependent cell adhesion…

Q: Please help! Sketch a titration curve of the peptide Ala-Tyr-Gln-Met-Asp-His from pH=0 to 14 up to 5…

A: Titration is used to determine the amount of acid in a solution.Sodium hydroxide or potassium…

Q: Which among the several mechanism below applies to the enzyme phenylalanine hydroxylase? A.…

A: B. Activation by phenylalaninePhenylalanine hydroxylase is activated by its substrate,…

Q: Determine whether each of the amino acids is polar, nonpolar, positively charged, or negatively…

A: Amino acids are fundamental building blocks of life. They form the basic units that make up…

Q: Name the two most common atoms hydrogen bonds within biological systems that give hydrogen a partial…

A: Hydrogen bond is formed between a hydrogen atom which is bonded to an electro negative atom( donor)…

Q: Total number of H-bonds formed by water molecules in 'liquid' state are Between 3 to 4 02 3

A: We need to identify the total number of hydrogen bonds formed by water molecule in its liquid state.…

Q: Calculate either [H3O+] or [OH-] for each of the solutions at 25 °C. Solution A: [OH¯] = 1.43 × 10¯7…

A: To calculate [H3O+] and [OH-] for each of the solutions, we can use the equation for the ion product…

Q: Among the given organelles, which ones are present or prominent in plant cells but not in animal…

A: Lysosomes;- are present in the cell of animal and they are responsible for breaking down waste and…

Question

A major difference between protein and DNA is that DNA has the same double-stranded structure
no matter what the content or order of the nitrogenous bases, but proteins have a different shape
depending on the content and order of the amino acids. Evolution has led to proteins that fold into
precise shapes, whether globular, tubular, fibrous, spherical, or netlike, based on how the polypep-
tide chain folds. It folds a bit at a time, making and breaking molecular interactions as it folds.
To describe these shapes, the four levels of protein structure were named primary, secondary,
tertiary, and quaternary.
The interactions formed in a protein as it is synthesized and then as it folds are the peptide
bond, the hydrogen bond, ionic bonds, polar interactions, disulfide bonds, and hydrophobic
interactions.
In the following chart, match each level to the interaction types that form it and to the
protein motifs or features generally ascribed to it. The possible interaction types and motifs to
choose from are listed in the boxes following the chart.
LEVEL
Primary
Secondary
Tertiary
Quaternary
Interaction Types
■ Disulfide bond
Hydrogen bond
Hydrophobic interaction
▪ lonic bond
Peptide bond
Polar interaction
INTERACTION TYPE
MOTIF/FEATURE ASCRIBED TO THAT LEVEL
Motif/Features Ascribed
. a-helix
. B-sheet
▪ B-turn
. Barrel
. Fold
▪ Hexameric structure
. Overall 3D shape
■ Polypeptide chain
. Protein domain
• Tetrameric enzyme

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

SEE SOLUTION Check out a sample Q&A here

Step 1: Protein structure

Step 2: Table

Step 3: Levels

Solution

Step by step

Solved in 4 steps

SEE SOLUTION Check out a sample Q&A here

Similar questions

To build a nucleotide, let's first consider the nitrogenous bases. A pyrimidine has one six-membered ring of carbon and nitrogen atoms. The members of the pyrimidine family are cytosine (C), thymine (T), and adenine (A). O TRUE O FALSE
The conditions on early earth were considered very harsh, volcanoes, lighting discharges, radiation, etc. However, we still are able to conceive the possibility that life may have arisen and existed under such harsh primitive conditions. The existence of organisms in extreme environments such as high acidity, salt, temperatures, etc even today supports the above possibility in conjunction with the theory of Darwinian evolution. O True False
It is often the case that a helices are positioned in a protein such that one side faces the interior of the protein and the other, the surface of the protein. These are said to be amphiphilic helices because they face different environments. Using a helical wheel projection (shown below), which of the peptide(s) below might form an amphiphilic helix? 8 15 1 12 4 11 16 18 9 7 14 13 10 17 O SLIKSVIEMVDEWFRTFL O FLIRVLRKVFRVLTRILS O RLFRSRVLKIAVIRFLLI
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 Cys
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
In class we learned about the H-bonding pattern in an alpha-helix. Asp 61 of the spidroin CTD has a slightly unusual H-bonding feature within the helix. That is because it forms three H-bonds. They are H-bonds between its carbonyl oxygen and , between its amide hydrogen and , and between its side chain and Hint: by clicking once on the ribbon diagram at any spot, the model will show H-bonding in that spot.
Which of the following is not correct regarding protein domains or modules such as the immunoglobulin domain, growth factor domain, and fibronectin domain? each type of domain is found in a variety of proteins O they always have the same function in differend proteins O domains are hypically 40 to 100 amine acids in length O they can be present in multiple copies in the same protein domains of a certain type usuaily have the same tertiary structure
How many amino acids are present on the helix to the right? Any partially drawn amino acids count as one whole amino acid Circle one peptide bond and box one R group on the figure to the right Describe how a lack of Vitamin C in the diet will affect the overall structure of collagen. Figure 6-7 Illustration, Irving Gels. Image from the Irving Geis Collection/Howard Hughes Medical Institute. Rights owned by HHMI. Reproduction by permission only. Drotoinc
Which of the following best describes how the secondary structure of a protein is formed? A B с D O=U a-helix H O=C N-H R-C-H C=0 H-N H-C-R O=C N-H R-C-H C=O H-N O-C N-H R-C-H C=O H-N N-H 0= H-C-R H-N C=O R-C-4 N-H O=C H-C-R 4-1 Ç=O R-C-H N-H 0=C H-C-R (=O R-C-H B-pleated sheet ionic bonds between the R groups of the polypeptide amino acids -Uh hydrogen bonds between the carboxyl and amino groups of non-adjacent amino acids covalent bonds between the carboxyl and amino groups of adjacent amino acids hydrogen bonds between the R groups of the polypeptide amino acids
The structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond towards the C-terminal end of the helix while the hydrogens of the NH groups orient toward the N-terminal end, thus imparting a dipole along the length of the helix. As a result, which kinds of amino acids would favor the C-terminal end, and which would favor the N-terminal end? negatively charged, positively charged positively charged, negatively charged negatively charged, hydrophobic positively charged, hydrophobic hydrophobic, negatively charged hydrophobic, positively charged
Which of the following is/are the fundamental difference/s between RNA and DNA? O the sugars only O bases, ribose units, and the phosphodiester linkage O bases, ribose units, and the glycosidic bond type bases and the ribose units only
Draw beta sheet with backbone hydrogen bonds, is this structure on the interior or exterior of the protein and why? Region 1: -Ser-Thr-Glu-His- Region 2: -Asp-Tyr-Lys-Asn