true/ false: When proteins are denatured 1°, 2°, 3°, and 4° structure is lost.
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true/ false: When proteins are denatured 1°, 2°, 3°, and 4° structure is lost.
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- Mass spectrometry and X-ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X-ray diffraction, or both techniques. Mass spectrometry protein must be conformationally stable X-ray diffraction small amounts of protein are sufficient analysis requires information about the protein-coding gene or genes Answer Bank protein may be denatured requires a large amount of protein protein sample must be pure can detect a covalent modification to a protein Both techniquesThe disulfide bonds that make up the tertiary structure of proteins are stabilized by hydrogen bonds. Select one: True FalseThe protein will lose its conformation when denatured by some factors such as a big change in pH and this will lead to the loss of protein function even when the denaturing agent is removed. Select one: O True O False
- By increasing the percentage of acrylamide in an SDS-PAGE gel, one will observe the following change in the range of molecular weights of the observed proteins. Decreased range of molecular weights observed. No change in range of molecular weights observed. Increased range of molecular weights observedPhysical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryo electron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?Quaternary structure defines the spatial arrangement of proteins with at least two polypeptide chains. True False
- Describe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.Physical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryoelectron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?The protein's secondary structure provide the overall arrangement of atoms. True or false
- Protein solubility in aqueous solutions is independent of ionic strength of the solution. True or FalseIn general, proteins can be classified into 3 different groups. Name and give a short description of each type and how they are distinct from one another. Provide an example of macromolecule or other complex structure representing each of the three types.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
