vas seconds ago E E Image options Replace image- . 4 6. A protein molecule composed of a sequence of polar amino acids, shown in blue, and a sequence of nonpolar amino acids, shown in pink is shown schematically below. How might you expect this protein to be located in the several phospholipid structures shown below? Choose all reasonable structures. 田回 !!!

vas seconds ago E E Image options Replace image- . 4 6. A protein molecule composed of a sequence of polar amino acids, shown in blue, and a sequence of nonpolar amino acids, shown in pink is shown schematically below. How might you expect this protein to be located in the several phospholipid structures shown below? Choose all reasonable structures. 田回 !!!

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Chemistry 1. how many amino acids is present in myosin (cite your sources) 2. Structure Characteristics/ Description (indicate for e()xample: amino acids number, type of secondary structure present such as alpha-helix or beta-pleated sheets) of myosin (cite your sources)
A. Amino Acids with Electrically Charged Side Chains Negative Pesitive Aspartie Acid Glutamie Acid (Asp D Lysine Histidine Arginine (Argl ® (Glul O (His H HO Ho HO -NH, -NH, NH, NH, -NH, NH NH H,N- ONH, ONH, C. Special Cases B. Amino Acids with Polar Uncharged Side Chains Proline Asparagine (Aan N Cysteine (Cya) © Glycine (Gly O Threonine Glutamine (Pra) P Serine (Ser 9 Но Họ Ho Ho Ho Но NH, NH, NH NH, NH, NH, -NH, но- SH он NH, NH, D. Amino Acids with Hydrophobic Side Chains Leucine (Leu O Phenylalanine (Phe e Tryptophan (Tp W Tyrosine Methionine Valine Isoleucine Alanine (Ala A IMe M Ho Ho Ho Ho HO NH, -NH, Но -NH, HO NH, NH, NH, NH, NH, NH он If the chromatogram was developed from reverse phase conditions, which of the following amino acids is expected to elute first? serine phenylalanine tryptophan O tyrosine
Amino Acids and Proteins 1. What are the structural features of amino acids with an emphasis on essential amino acids? 2. Write the properties of amino acids: zwitterion, pka, pKb, amphoteric character, isoelectric point, and electrophoresis. 3. Write the mechanism of peptide bond formation and what are its structural features. 4. What are the different types of proteins and their function? 5. Explain the meaning and importance of the primary, secondary, tertiary, and quaternary structures of a protein and the factors that cause its denaturation.
Use the online JPRED 4 secondary structure prediction tool (Pred: A Protein Secondary Structure Prediction Server (dundee.ac.uk) to predict the secondary structure for the following input sequence: MNLVLMGLPGAGKGTQAEKIVAAYGIPHISTGDMFRAAMKEGTPL GLQAKQYMDRGDLVPDEVTIGIVRERLSKDDCQNGFLLDGFPRTV AQAEALETMLADIGRKLDYVIHIDVRQDVLMERLTGRRICRNCGAT YHLIFHPPAKPGVCDKCG GELYQRADDNEATVANRLEVNMKQMK PLVDFYEQKGYLRNINGEQDMEKVFADIRELLGGLAR How many helical regions are predicted? (Hint: see the View Simple Results in HTML). A 4 B 6 C O D 8 E 1
Write the structure of all possible peptides containing these amino acids: Ala, Leu, Use single letter abbreviations and capital letters only; i.e. GYR, not Gly-Tyr-Arg. If there are fewer than 6 peptides, leave an appropriate number of answer boxes empty.
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the amino acid is tryptophan
Q3- We wish to synthesize all possible dipeptides containing the amino acids tyrosine, lysine, phenylalanine, and leucine. Identify the number of possible dipeptides and explain how we would carry this out using combinatorial techniques.