The molecule I was given is picene: and I need to answer this question 1. You will treat your 2D Pi electron system as an 2D particle-in-a-box of width Lx (theshorter x dimension) and length Ly (the longer y dimension) - where for convenienceyou will orient the molecule so that length Ly is the long axis. Using the aromatic bondlength of 1.42 Å and simple geometry, calculate the width and length of your molecule.

To calculate the width (Lx) and length (Ly) of the molecule picene using the aromatic bond length of…

Answered: 1. You will treat your 2D Pi electron…

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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H OH CH2OH D H ОН H الحزن ОН CH2OH ОН H ОН I Which of the following statements correctly describes this structure? (A) The monomer units are bonded by beta 1-2 glycosidic linkage. B The monomer units are bonded by alpha 1-2 glycosidic linkage. The monomer units are bonded by alpha 1-4 glycosidic linkage. The monomer units are bonded by beta 1-4 glycosidic linkage. H CH2OH H ОН H ОН H ОН
2. You have 15mL of a 0.3M solution of His-Lys-Leu-Asp adjusted to pH=9. You titrate your solution with 10mL of 0.2M HCl. Relevant pka values are 2.1,3.8,6.0,9.8 and 10.5. A) Draw the structure of the tetrapeptide that predominates in solution before you add any HCl. B) Calculate the new pH value of the solution after the addition of HCI. C) You digest this tetrapeptide with trypsin at pH=( and apply the products to an anion exchange column. Write the amino acid sequence of the products that are produced. If you gradually add HCl to the column, in what order will these products elute, if at all?
Consider the structure shown below. он 3 5 CH; O CH, O H CH; O 1 H-N-CH,-C-N-CH;-C-N-CH-C-N-CH-C-N-CH-C-ơ 2 H. H H Fill in the blank with an integer (1, 2, 3, 4, 5..) as shown in the diagram or to represent a specified number. A hydrophilic side chain is indicated by the number
GenAlex Medical, a little-known division of a major Swiss pharmaceutical firm, recently developed a new synthetic steroid S. Their patent application describes S as "made from a steroid nucleus with hydroxyl groups at positions 3 and 7, and methyl groups at positions 4 and 12." In the drawing space below, draw the chemical structure of S. If more than one structure is possible, you can draw any of them. Click and drag to start drawing a structure. ח' G c E
Draw the structure and name the following polypeptides: 1. SRAL b. ENIRYTAK
Stereochemistry in biological molecules is often denoted by the D- and L- convention, instead of the R- and S- configurations determined by the Cahn-Ingold-Prelog methodology. Naturally occurring α-amino acids are typically in the L-configuration. The Fischer projection of L-alanine is shown. L-alanine H₂N- H3C- HOOC Identify which structures are equivalent to the L-configuration. H COOH H CH3 NH₂ -COOH NH₂ CH3 -H CH3 COOH H -NH₂ H₂N- H CH3 COOH NH₂ H CH3 -COOH
Sketch the MO diagram for 1,3 budadiene. Determine the net bonding interactions for ¥2 and ¥3. How many nodes are in ¥4? How many AO’s were used? How many MO’s resulted?
Now consider alanine as a whole molecule. Use the Ka values from the chart above, and your understanding of the relationships among Ka, pH, and charge to select the predominant form of alanine that would exist at the pH indicated below. Note some choices may not be used and some may be used more than once. А. CH3 В. CH3 С. CH3 NH3+ C СООН NH2 C COOH NH2 C CO- - H H. D. CH3 Е. CH2- F. CH2- NH3+ - C СО- NH2 CO- NH2 СООН - C - H H. pH = 1 [ Choose ] pH = 5 [ Choose ] pH = 7 [ Choose ] pH = 11 [ Choose ] > > >
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal –NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys–Pro–Val–Gly–Lys–Lys–Arg-Arg-Pro-Val-Lys–Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-GIn– Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Ala-Pro-Val-Gly-Glu-Glu–Cys-Asp-Pro-Val-Glu–Val–Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu–His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val–Gly–Glu-Glu-Cys-Asp-Pro–Val-Glu–Val–Tyr-Pro-Asp-Ala (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu-Val-Tyr-Pro-Asp- Lys–Ala-Gly-Arg-Glu-Ser-Arg-Ala (d) Which of the three peptides would migrate the closest to the anode in isoelectric focusing? (e) Which of the above peptides would elute last from a gel filtration column? (f) Which of the three…
Draw the structure of predominant ionic species and also predict the net charge for Following oligopeptides at pH 7.0. [A] Trp-Lys-Asp
The twisted proteins store elastic potential energy as it twists or untwists from its equilibrium state. The energy function for this system is shown in the figure where the energy is given in multiples of kBT which is a unit of energy used by biochemists when working at the molecular level. (1.0 kBT = 4.11×10−21 J). Figure 6 shows a horizontal line at an energy level of 136 kBT , which gives a total angular range of 2.095 radians. If the energy level of the ATP-synthase stalk is 100 kBT instead, between what angles is the stalk confined? Explain your reasoning.
Now consider alanine as a whole molecule. Use the Ką values from the chart above, and your understanding of the relationships among Ka, pH, and charge to select the predominant form of alanine that would exist at the pH indicated below. Note some choices may not be used and some may be used more than once. А. CH3 В. CH3 С. CH3 NH3+ C COOH NH2 COOH NH2 CO- - - H H D. CH3 Е. CH2- F. CH2- NH3+ C CO- NH2 CO- NH2 СООН H H H pH = 1 A pH = 5 D pH = 7 pH = 11 C >

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