Exam 3: Protein Structure and Function
Exam 1: Chemical Foundations42 Questions
Exam 2: Molecular Genetic Techniques50 Questions
Exam 3: Protein Structure and Function51 Questions
Exam 4: Culturing and Visualizing Cells36 Questions
Exam 5: Fundamental Molecular Genetic Mechanisms50 Questions
Exam 6: Bio-membrane Structure37 Questions
Exam 7: Genes Genomics and Chromosomes48 Questions
Exam 8: Transcriptional Control of Gene Expression51 Questions
Exam 9: Post-Transcriptional Gene Control49 Questions
Exam 10: Transmembrane Transport of Ions and Small Molecules44 Questions
Exam 11: Cellular Energetics51 Questions
Exam 12: Moving Proteins Into Membranes and Organelles41 Questions
Exam 13: Vesicular Traffic, Secretion, and Endocytosis39 Questions
Exam 14: Signal Transduction and G-Protein Coupled Receptors45 Questions
Exam 15: Signaling Pathways That Control Gene Activity43 Questions
Exam 16: Cell Organization and Movement I: Microfilaments46 Questions
Exam 17: Cell Organization and Movement II: Microtubules and Intermediate Filaments43 Questions
Exam 18: Regulating the Eukaryotic Cell Cycle41 Questions
Exam 19: Integrating Cells Into Tissues44 Questions
Exam 30: Cell Birth, Lineage, and Death39 Questions
Exam 21: Nerve Cells43 Questions
Exam 22: Immunology42 Questions
Exam 23: Cancer43 Questions
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GTPases serve in many signal transduction pathways and the presence of GTP or GDP dictates whether the pathway is on or off,respectively.Which of the following statements is true regarding guanine nucleotide exchange factors (GEF)and their role in these signaling pathways?
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(Multiple Choice)
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Correct Answer:
C
The Km for an enzyme-catalyzed reaction:
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(Multiple Choice)
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Correct Answer:
C
The conversion of inactive chymotrypsinogen to active chymotrypsin is an example of:
(Multiple Choice)
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Proteases that attack selected peptide bonds within a polypeptide chain are synthesized and secreted as inactive forms called:
(Multiple Choice)
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Describe the general mechanism by which a multisubunit protein can be activated by binding an allosteric effector molecule.
(Essay)
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All the following statements about molecular chaperones are true EXCEPT:
(Multiple Choice)
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Mass spectrometry techniques are used in proteomics for all of the following purposes EXCEPT:
(Multiple Choice)
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What types of bonds are apt to be more common in the nonaqueous,interior environment of a protein than in the aqueous,surface environment of a protein?
(Essay)
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How can gel filtration chromatography separate proteins based on their mass?
(Essay)
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What role does aberrant protein folding play in the development of a disease such as Alzheimer's disease?
(Essay)
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Eggs are protein-rich foods.An uncooked egg can catalyze a reaction that breaks down bacterial cell walls.After cooking,this activity is almost abolished.This is likely because:
(Multiple Choice)
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In two-dimensional gel electrophoresis,proteins are first resolved by _____ and then by _____.
(Multiple Choice)
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You disrupt all hydrogen bonds in a protein.What level of structure will be preserved?
(Multiple Choice)
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A small molecule that binds directly to the active site of an enzyme and disrupts its catalytic reaction is called:
(Multiple Choice)
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Describe the types of bonds/interactions that hold together or stabilize the primary,secondary,tertiary,and quaternary structures of proteins.
(Essay)
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Modification of proteins by ubiquitin and ubiquitin-like E3 ligases can stimulate all of the following EXCEPT:
(Multiple Choice)
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