Suppose you are researching a new protein and find that the shape of the protein yields little information as to its function. What would you look at next to try and understand more about it? A. The tertiary structure B. the primary structure to determine the order and behavior of r groups C. the secondary structure

Suppose you are researching a new protein and find that the shape of the protein yields little information as to its function. What would you look at next to try and understand more about it? A. The tertiary structure B. the primary structure to determine the order and behavior of r groups C. the secondary structure

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter2: Chemistry Of Life

Section: Chapter Questions

Problem 7RQ: Describe the four levels of protein structure. How do a proteins side groups influence its...

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ion 65 A group of biologists developed a drug that target a specific protein and inhibit its function. This drug cuts the bonds between strongly positive and strongly negative sides of the protein. Which level of protein structure would be affected directly by this drug? et ered ed out of Select one: uonsənb 61 O a. Quaternary structure O b. Secondary structure Oc. Tertiary structure O d. Primary structure e. B pleated sheet
Biochemists talk about protein structure at four distinct levels: primary, secondary, tertiary and quaternary structure. Below are depictions of each of these levels of protein structure. For each image, match the term and the written description of the level of protein structure that the image depicts. Drag the appropriate items to their respective bins.
What is one of the determining factors in the three-dimensional structure of a protein? A.The location of alpha sheets and beta propellersB.The presence of another proteinC.The location of hydrophobic and hydrophilic amino acidsD.The presence of nucleic acids such as DNA
In a protein, a mutation occurs and results in phenylalanine being replaced by an alanine. This would. Select one: a. Always change the primary structure of the protein, never change the tertiary structure of function. O b. Always change the primary structure of a protein, sometimes affect tertiary structure and function. c Never change the primary structure, always affect secondary and tertiary structure and function. O d. Sometimes change the primary structure of a protein, always affect the tertiary structure, and sometimes affect function.
Draw an amino acid sequence and identify peptide bonds or which atoms will hydrogen bond with each other in secondary structure. (Could you explain secondary structure also?)
Which of the following is incorrect concerning protein structure determination by X-ray crystallography? Choose one: O A. X-ray crystallography provides dynamic information about protein structure. O B. A 1.5 Å resolution structure is better than a 3 Å resolution structure. O C. Isomorphous replacement is used to aid phase determination. O D. Highly ordered crystals are required.
In studying a particular biomolecule (protein, nucleic acid, carbohydrate, lipid), a biochemist needs to separate/ purify it from other biomolecules in the sample. However, looking at the monomeric subunits of a biomolecule, one should have an idea about the characteristics of the molecule that would allow to separate/purify it from other molecules. On what basis can you separate: a. amino acids from fatty acids? b. nucleotides from glucose?
Large globular proteins frequently are comprised of two or more recognizable structures that often confer unique functions or properties. These structures are termed: a quatemary structure b. domains c. heterotropic d. multimeric e à ande
In order to study protein structures and functions, many protein techniques have been developed for specific applications. Which of the following pair of technique: application is INCORRECT? a. Mass Spectrometry: protein molecular weight b. SDS-PAGE: protein structure c. X-ray crystallography: protein structure d. NMR: protein structure e. Peptide mass fingerprinting: protein presence and identification
Denaturation is the loss of protein function from structuralchange or chemical reaction. At what level of proteinstructure or through what chemical reaction does each ofthe following denaturation agents act?a. heatb. strong acidc. saturated salt solutiond. organic solvents (e.g., alcohol or chloroform)
How does knowledges of protein structure help us to predict the function of unknown proteins?
How does the coplanar nature of the peptide bond impact the overall structure of a protein? O a. It facilitates the stacking of aromatic side chains. O b. It promotes the flexibility of the protein backbone. Oc. It restricts the formation of secondary structures. Od. It allows for the easy formation of disulfide bonds. It constrains the rotation around the peptide bond, influencing protein folding.