Fluorescent proteins like the green fluorescent protein (GFP) found in jellyfish are a class of colorfulproteins that shine a particular color when exposed to ultraviolet light. These proteins, despiteexhibiting a wide range of diverse colors, have nearly identical secondary structure across organismsand phenotypes. Each GFP-like protein has a few alpha-helices as well as a characteristic beta-barrecomposed of 11 beta-sheets that shields the inside of the protein from solvent (i.e., water). The GFPlike protein shown below is a green fluorescent protein from the great star coral Montastraeacavernosa and contains two alpha-helices in its structure (labeled A and B and colored cyan).A1. Helix A contains 6 amino acids, including a phenylalanine and an aspartic acid. Which position (1or 2, colored in red) would you more likely expect aspartic acid to be located?[ Select ]2. If you were to compare helix A to helix B, would you expect the ratio of polar:non-polar residuesto be higher or lower in helix B?[ Select]

Proteins are composed of different types of amino acids (polar charged, polar uncharged, and…

Answered: Fluorescent proteins like the green…

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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Similar questions

Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.
Most animals cannot use wool for nourishment. An exception is the clothes moth: it can derive nourishment from eating clothing made of natural fibers such as wool (which is rich in a-keratin). The digestive tract of the larvae of clothes moths provides a highly reducing environment. Why is this beneficial to the larvae? The reducing environment will reduce the disulfide linkages, making it easier to digest the proteins. The reducing environment will hydrolyze the peptide bonds. The reducing environment will interfere with the H-bonding between the tropocollagen molecules, making the type of protein found in most natural fibres easier to digest. The reducing environment will help to kill bacterial pathogens. The reducing environment will detoxify the carcinogenic dyes used in the textile industry.
Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a negatively charged carboxyl group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structure
The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in the solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface do. Determination of these rates can be used to explore the proteinfolding reaction, probe the tertiary structure of proteins, and identify the regions of protein–protein interfaces. These exchange reactions can be followed by studying the behavior of the protein in solvent that has been labeled with deuterium ( ²H), a stable isotope of hydrogen. What two methods described in this chapter could be readily applied to the study of hydrogen– deuterium exchange rates in proteins?
a) The pl of a protein is 9.0. What will be the net charge (positive, negative or neutral) on the protein under the following conditions: A buffer with pH 9.0: A buffer with pH 7.0: A buffer with pH 10.0: b) Your protein is present in a sample buffer which has a pH 7.0. The sample is applied to an ANION EXCHANGE column. Will protein 1 bind to the beads on the column? Yes/No
You have discovered a novel protein that has a pl = 5.5. To study the functional properties of this new protein, your research group has made a mutant that contains two amino acid changes: a surface phenylalanine residue in the normal protein has been replaced by histidine (side chain pK, = 6.1), and a surface glutamine has been replaced by glutamic acid (side chain pK, = 6.0). Is the pl of the mutant protein predicted to be greater than, less than, or the same as the pI of normal protein? Support your answer with the appropriate calculation.
Draw a hydropathy plot and a 2D protein cartoon for a protein that passes through the lipid bilayer 6 times..
Which of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%
A protein of unknown structure has been purified. Size-exclusion chromatography reveals that the native protein has a MW of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of MW 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM B-mercaptoethanol yields peaks for proteins of MW 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
You've isolated a novel protein, but you believe what you actually have is a mixture of the unmodified and phosphorylated protein. Which of these methods would be best for helping you to determine if you do indeed have a mixture of phosphorylated and non-phosphorylated protein, while also establishing other vital characteristics of this novel protein? O 2D-PAGE O SDS-PAGE O Isoelectric focusing O Native-PAGE
Proteins function in a variety of roles in the body. The 3 main categories are: Growth and Maintenance, Regulatory Roles, and Energy Production. Please provide 2 examples of Growth and Maintenance and 4 examples of Regulatory Roles

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