1. Draw the general structure of glycerophospholipids and designate the site for variation in head group.LIPID NAMESTRUCTUREPhosphatidic acidPhosphatidylethanolaminePhosphatidylcholinePhosphatidylserinePhosphatidylglycerolPhosphatidyllinositol

Lipids are non-polar hydrocarbons, like fatty acids (FA), waxes, sterols, fat soluble vitamins (A,…

Answered: 1. Draw the general structure of…

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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Explain the differences in the ease of lateral movement and bilayer translocation movement of phospholipids.
Explain how membrane lipids self-assemble into bimolecular sheets.
4. In the following diagram of a portion of a protein, label the types of interactions that are shown. CH H;Ć `CH, | H;C _CH3 ! CH - Polypeptide backbone c=OH CH2 -CH5–S}-CH,-- -CH;-CH-CH;-CH, NH," 0-C-CH, d. What level of protein structure are these interactions producing?
10. Which of the following statements is FALSE about proteins? A) The sequence of the atoms in the polypeptide backbone does not vary between different proteins. BYProteins would fold to the most stable conformation with the lowest energy level. C) Misfolded protein can be sent to the proteosome where they will be folded into the correct conformation. DY The three-dimensional structure of a protein is in general determined by the sequence of the amino acids. E) Proteins are linear polymers built of amino acids.
7. What level of protein structure is retained when proteins unfold? Using what you know about the different bonds holding protein structure together, explain why this level of protein structure is retained when the protein unfolds. 15
9. Look at the protein below. Label the diagram on the right and show which part of the protein has hydrophobic amino acid residues and what part of the protein has hydrophilic amino acid residues. Explain how you know.
17. please check
Write 2 (any) functions of membrane carbohydrates and explain the functions.
8. A dipeptide T, obtained from the breakdown of an enzyme found in the human body, is made up of Amino Acids R and S. (a) Classify Amino Acids R and S as an acidic amino acid or a basic amino acid. (b) Name Bond Q. (c) State any ONE type of protein that could be found in human body. (2%) (1%) (1%)
Explain the different properties of the head and tails of phospholipids (polar, hydrophilic, nonpolar, hydrophilic)
1) Placing phospholipids in water will spontaneously form a spherical structure called a:Group of answer choices lumen ball sphingoid cytoskeleton liposome 2) Saturated fatty acidsGroup of answer choices Have each carbon "saturated" with hydrogen Have each carbon "saturated" with other carbons Have each carbon "saturated" with hydrogen and are solids at room temperature Are solids at room temperature Contain double bonds 3) In intestinal epithelia, glucose can be taken into cells against its concentration gradient. How can glucose be transported against its concentration gradient without the direct expenditure of ATP in intestinal epithelial cells?Group of answer choices It uses simple diffusion It uses the Glut1 transporter It uses the Glucose ATPase It uses the Glucose/Na+ symporter None of the above. Due to the Second Law of Thermodynamics, molecules cannot be moved against their concentration gradient.
1. Most globular proteins are denatured and lose their activity when briefly heated to 65°C. However, globular proteins that contain multiple disulfide bonds often must be heated longer and at higher temperatures to denature them. Furthermore, upon cooling of the denatured proteins, the activity of these proteins can often be restored. Explain these properties.

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