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The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in a solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface. By determining these exchange rates, we can explore protein-folding reactions, probe the tertiary structure of proteins, and identify the regions of protein-protein interfaces. We can investigate these exchange reactions by studying the behavior of the protein in solvent that has been labeled with deuterium, 2H, a stable isotope of hydrogen. Select the methods that could be readily applied to the study of hydrogen-deuterium exchange rates in proteins. enzyme-linked immunosorbent assay (ELISA) nuclear magnetic resonance (NMR) spectroscopy x-ray crystallography mass spectrometry (MS)

The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in a solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface. By determining these exchange rates, we can explore protein-folding reactions, probe the tertiary structure of proteins, and identify the regions of protein-protein interfaces. We can investigate these exchange reactions by studying the behavior of the protein in solvent that has been labeled with deuterium, 2H, a stable isotope of hydrogen. Select the methods that could be readily applied to the study of hydrogen-deuterium exchange rates in proteins. enzyme-linked immunosorbent assay (ELISA) nuclear magnetic resonance (NMR) spectroscopy x-ray crystallography mass spectrometry (MS)

Biochemistry
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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The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in a solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface. By determining these exchange rates, we can explore protein-folding reactions, probe the tertiary structure of proteins, and identify the regions of protein-protein interfaces. We can investigate these exchange reactions by studying the behavior of the protein in solvent that has been labeled with deuterium, 2H, a stable isotope of hydrogen. Select the methods that could be readily applied to the study of hydrogen-deuterium exchange rates in proteins. enzyme-linked immunosorbent assay (ELISA) nuclear magnetic resonance (NMR) spectroscopy x-ray crystallography mass spectrometry (MS)
Transcribed Image Text:The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in a solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface. By determining these exchange rates, we can explore protein-folding reactions, probe the tertiary structure of proteins, and identify the regions of protein-protein interfaces. We can investigate these exchange reactions by studying the behavior of the protein in solvent that has been labeled with deuterium, 2H, a stable isotope of hydrogen. Select the methods that could be readily applied to the study of hydrogen-deuterium exchange rates in proteins. enzyme-linked immunosorbent assay (ELISA) nuclear magnetic resonance (NMR) spectroscopy x-ray crystallography mass spectrometry (MS)
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