|| Biological Molecules-Modelling Activity AC1.1-ustrate or construct molecular models of simple arganic compounds. Using the key shown, illustrate the biological molecules that are named below: Alpha Glucose Key Single Bond O Hydrogen Double Bond Oxygen Nitrogen Glycerol Glycine (r=H) Foc
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- Question 13 of 40 0% Identify the true characteristic of glutamate at its isoelectric point (pI). 00% The net charge of glutamate is positive. prrect The side chain of glutamate has a negative charge. L00% In an electric field, glutamate migrates toward the anode. orrect The net charge of glutamate is zero. 0% In an electric field, glutamate migrates toward the cathode. 0% Determine the pl of glutamate given its pK at each charge state. Give your answer to two decimal places. Progress Charge: 1+ 1- 2- 0% H,N- CHCO, CH, *H,N-CHCO,H *H,N-CHCO, *H,N–CHCO, CH, CH, pK = 9.67 CH, CH, pK = . = 4.25 0% pk = 2.19 CH, CH, CH, C=0 C=0 C=0 Ć=0 0% MacBook Pro Q Search Default Search &Only qno3m I think protein drawing has to show the bond interactions Onlyqno3 solve. I. Given a polypeptide below, answer the following questions: MAGGMIVIIGGMGCNSMVVVIIIGTSSCVIMEMMMIVKII Questions: 1. Enumerate all non-polar amino acids. (Provide the single letter and common name) 2. Enumerate polar amino acids include the acidic and basic types. (Provide the single letter and common name) 3. Illustrate the overall shape of the given polypeptide. Point out the specific side-chain interactions that could occur in this polypeptide by labelling the polypeptide. Defend your answer as to why your polypeptide should assume such final shape. Only accurate drawing needEnter numerical values only as you complete the following fill-in-the blanks. The amino acid aspartate has 3 - has a charge range of 1 from fully protonated to fully deprotonated) Ⓡ - -2 ionizable protons and At pH of 7.4, the net charge of the amino acid aspartate is_ -1 . (go
- [Ten - Biomolecules] INSTRUCTIONS — Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer. — Answer properly Questions; Thomas was purifying an enzyme from a homogenate of muscle cells. He went through seven steps of purification and found that the enzyme activity was the same as the homogenate value. On the eighth step, when the protein washighly pure, the enzyme activity rose to five times that of the homogenate value. Can you suggest a possible reason? A. the homogenate assay was wrong B. step eight has co-purified an activator of the enzyme. C. the enzyme has an inhibitor present in the muscle cell homogenate D. the temperature at step eight was just right for the enzyme activity.Explore the difference etween amylopectin and glycogen. Be sure to highlight what structural modifications in the molecules as it relates to their localization in different organisms (structure-function relationship).Protein,nfolded Proteinţolded Under certain conditions, a specific protein has the following thermodynamic parameters for going from the unfolded state to the folded state: AH = – 300 kJ/mol, and TAS = – 400 kJ/mol. Under those conditions, the equilibrium would lie more toward neither would predominate - the fraction of total protein that's folded would = fraction unfolded. the folded state the unfolded state O It is impossible to predict the position of the equilibrium from AH and TAS.
- age 2 of 9 FI 1. Recognize the following types of biomolecules when given images such as the ones below and on the next page: ● glucose (which is a monosaccharide) HO 0 of 618 words F2 ● ● ● amino acid protein (recall a protein with less than 50 amino acids can also be called a peptide whereas a protein with 50 or more amino acids can also called a polypeptide) steroids polysaccharide ● • triglycerides ● ● phospholipids ● ● DNA RNA CH₂OH H OH H H OH English (United States) 20 F3 $ +: OFF Draw with Add Pen Trackpad 000 % F5 MacBook Air A DNA F6 & ◄◄ F7 * ► 11 F8 Focus F9 R F10 - F11 21246 2 H 8 Is M (n Ge M In In VI LE Q s M In b M 7 x + uv A canvas.northseattle.edu/courses/2086259/quizzes/5876542/take (a) Saturated fatty acid (b) Unsaturated fatty acid Account Dashboard Palmitic acid Linoleic acid 200L anauer Aemciates Ine. Courses Shown here are examples of saturated and unsaturated fatty acids. Explain what is meant by the term saturated fatty acid, and explain, at the molecular level, why Groups saturated fatty acids remain solid at higher temperatures than unsaturated acids do. Calendar Edit View Insert Format Tools Table В T? v: 12pt v Paragraph v U A Inbox History Help 8:18APPLICATIONS ON PROTEINS S TY Question #1: A shampoo bottle lists "partially hydrolyzed protein" as one of its ingredients. What is the difference between partially hydrolyzed protein and completely hydrolyzed protein? partially hydrolyzed protein completely hydrolyzed protein
- Search .l 7:15 AM < Вack Assignment #1-1.docx 34. The isomer of alanine shown below is one of the 20 naturally occurring amino acids that are used to make proteins. Amino acids like alanine exist at neutral acidity (pH = 7) in the following form: :0: H3C- NH3 35. What would be the structure of alanine if HCl(aq) was added to lower the pH = 1? What would be the structure of alanine if NaOH(aq) was added until the pH = 12? 36. Write an equation to show the reaction between ethanol, C,H,OH and methyllithium, CH,Li. Draw all non-bonding electrons and show electron flow with curved arrows. 37. Write an equation that shows the reaction between acetic acid (CH,COOH) and triethylamine (CH;CH,),N. Draw all non hondina lona elaotron naira ond chow the olootron flouu Dashboard Calendar Тo Do Notifications InboxA bconline.broward.edu/d21/le/content/466883/viewlontent/ Watch Miss caretak... Watch The Pet Girl... MyLabsPlus | Pearson New Tab ps O ADVANCED MATERIAL Identifying the important intermolecular forces in pure... Decide which intermolecular forces act between the molecules of each co intermolecular forces compound (check all that apply) dispersion dipole hydrogen-bonding hydrogen sulfide N2 nitrogen H, hydrogen water Explanation Check IINeed help The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer. HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys HbS: Val-His-Leu-Thr
