i need the answer quickly 1. Fact Check Match the following statements about protein struc-ture with the proper levels of organization.(1) Three-dimensional arrangement of all(a) Primarystructure(b) Secondarystructure(c) Tertiarystructure(d) Quaternarystructureatoms(2) The order of amino acid residues in thepolypeptide chain(3) The interaction between subunits inproteins that consist of more than onepolypeptide chain(4) The hydrogen-bonded arrangement of thepolypeptide backbone

The polypeptide chains are folded into their native conformations in order to become biologically…

Answered: 1. Fact Check Match the following…

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

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Check the TRUE alternative in relation to amino acids and proteins: (a) the precipitation of a protein is always an irreversible process (b) the isoelectric point of amino acids with non-ionizable side chain is reached at neutral pH (= 7) (c) all the amino acids that make up our proteins have a chiral carbon whose configuration is (S) (d) denaturation affects all structural levels of proteins (e) all amino acids are soluble in water and have relatively high melting points
. Assume that some protein molecule, in its folded native state, has one favored conformation. But, when it is denatured, it becomes a "random coil," with many possible conformations. (a) What must be the sign of AS for the change: native → denatured? (b) How will the contribution of AS for native → denatured affect the favorability of the process? What apparent requirement does this impose on AH if proteins are to be stable structures?
Part I. Protein structure You have the toy model for a protein in the water (W) environment of the cell shown. a) How many residues (amino acids) does this toy protein have? b) How many hydrophobic (H), hydrophilic (P), and charged (C) residues are there? c) Sketch the molecule on your answer sheet and then show the positions of the favorable C-C (charge-charge) interactions on the figure.
A/B: 3. Amino acid residues and peptide bonds (a) Draw the chemical structure of F, S and H joined by peptide bonds and also connected to neighboring residues as found in a protein. (b) Include all charges as expected at physiological pH (pH = 7.5) () Rank these three amino acid residues by hydrophobicity, pKa, and by nucleophilicity (d) For the central amino acid residue, identify the phi and psi dihedral angles by drawing a curved arrow indicating rotation about the chemical bond. (e) What group(s) eclipse each other if Phi = 0 degrees? Words and Pictures. (f) While Phi = 0 is not well tolerated, Psi = 0 is not uncommon, a so-called “allowed" but not most-favored region of the Ramachandran plot. What group(s) eclipse each other if Psi = 0 degrees and why is this less problematic than the situation created by Phi = 0. Words and Pictures H₂N* Pka: 9.13 H₂C с C._hydrophobicity: 1. phenylalanine (most) 2. Serine 3. Histidinelleast) ده H H. HIN OH I CH₂ CHO pka: 1. Serine (nighest) 2.…
. Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is true
2. Subunit Composition of a Protein. A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography ( F). When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (=), three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein. Note: dithiothreitol is a reagent to beak down the disulfide bonds.
. Suppose you have two genetic variants of a large protein that differ only in that one contains a histidine (side chain pk, = 6.0) when the other has a valine (uncharged side chain). (a) Which would be better for separation: gel electrophoresis or isoelectric focusing? Why? (b) What pH would you choose for the separation?
Protein Concept Map Add these terms to your concept map should include these concepts and details: Structure (functional groups, shape); Monomer; Linkage; Properties; Functions; Key terms from the Partial List of Key Terms from the Minds Partial List of Key Terms essential amino acid amino acid side group/R-group peptide bond polypeptide receptor neurotransmitter hormone secondary structure tertiary structure quaternary structure fair test hydrophobic hydrophilic intermolecular force of attraction
Exercise B: Peptide Bond Formation Figure 2 shows two individual amino acids, and then those same two amino acids after they have been linked together by a peptide bond to form a dipeptide. Addition of more amino acids linked by peptide bonds would form a polypeptide, the precursor to a functional protein. H H H. H H +| | H-N-Ċ- ċ-0 H-N-Ć- Ĉ-O H-N-Č -C. N-C-C- H CH2 H. CH2 H. CH2 H CH2 SH SH NH2 NH2 Figure 2. Formation of a peptide bond between two amino acids. Answer the below questions in your own document. F1. Which two amino acids are shown on the left side of Figure 2? Use the Figure They 3.2 from your text to answer this. 2. To which chemical groups do these amino acids belong? 3. Were you able to identify their chemical characteristics based on your rules? If not, you should go back and revise your rules! On the dipeptide shown in Figure 2, label the peptide bond that was formed when the two individual amino acids were joined. Label the free amino and carboxyl groups at the ends…
4. Amphiphilic Lipids. Detergents are small amphiphilic molecules that tend to form micelles in water. (a) Draw the structures of sodium dodecyl sulfate (SDS) and Triton X-100 (b) For each drawn detergent, indicate which portions (ends) of the molecules are hydrophilic and hydrophobic. Justify your answer (explain why hydrophilic vs hydrophobic). (c) Draw the micelle structure for one of the detergents. (d) Why does the detergent form a micelle and not a bilayer? Why do detergents denature proteins and remove grease from your clothing?
1. Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Suggestseveral features of proteins that drastically limit the actual number. 2. What are the greatest structural features that differentiate sphingolipids from phosphoglycerides? 3. High levels of glucose-6-phosphate inhibit glycolysis. If the concentration of glucose-6-phosphate decreases,activity is restored. Why?
Exercise B: Peptide Bond Formation Figure 3 shows two individual amino acids, and then those same two amino acids after they have been linked together by a peptide bond to form a dipeptide. Addition of more amino acids linked by peptide bonds would form a polypeptide, the precursor to a functional protein. нн H H O нно H O +| | || H-N-C-ċ-o + +| 1 || H-N-C-C +| | || Н-N—С- С—N—C—С H CH2 H CH2 H CH2 CH2 SH SH NH2 NH2 Figure 3. Formation of a peptide bond between two amino acids. Answer the below questions in your own document. • Which two amino acids are shown on the left side of Figure 3? Use Figure 2 to answer this. • To which chemical groups do these amino acids belong? Were you able to identify their chemical characteristics based on your rules? If not, you should go back and revise your rules! On the dipeptide shown in Figure 3, label the peptide bond that was formed when the two individual amino acids were joined. Label the free amino and carboxyl groups at the ends of this…

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