Biology

Biology, 03.11.2019 17:31, dontcareanyonemo

What happens to the functionality of a protein if the ph changes

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Biology, 21.06.2019 16:10, jroig42

Which of the following statements regarding anfinsen's denaturing experiments with ribonuclease a (rnase a) are valid? exposing the denatured protein to air oxidation and then dialysis to remove urea restored the protein to its original functionality. removing urea by dialysis and then allowing air oxidation of the denatured protein restored the protein to its original functionality. denaturing the protein with both urea and β-mercaptoethanol yielded an inactive protein. anfinsen concluded that protein folding is determined by its primary sequence.

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Biology, 12.07.2019 17:30, jadenp23

One consequence of protein denaturation is: a. the protein performs better than before. b. the protein adds another protein to its folded shape. c. the protein becomes more tightly folded. d. the protein forms covalent sulfur-sulfur bonds. e. the protein loses its functionality.

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Geography, 20.09.2019 23:00, zanestone12

1. describe the structure of a monosaccharide. 2. describe the structure of a disaccharide. 3. describe and draw the structure of a nucleotide. 4. where are nucleic acids found? 5. describe and draw the structure of an amino acid. 6. how can two molecules with the same chemical formula react differently? 7. describe the structure of a protein. 8. what is the role of an enzyme in a chemical reaction? 9. what happens to an enzyme once it catalyzes a chemical reaction? 10. what happens to the functionality of a protein if the ph changes? 11. what happens to the functionality of a protein if the temperature changes? 12. what is the relationship between the shape of an enzyme and the reactions they catalyze? 13. how does an enzyme inhibitor work?

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Chemistry, 27.09.2019 01:10, hella33revj

Which of the following statements regarding anfinsen's denaturing experiments with ribonuclease a (rnase a) are valid? exposing the denatured protein to air oxidation and then dialysis to remove urea restored the protein to its original functionality. removing urea by dialysis and then allowing air oxidation of the denatured protein restored the protein to its original functionality. denaturing the protein with both urea and β-mercaptoethanol yielded an inactive protein. anfinsen concluded that protein folding is determined by its primary sequence.

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