Acknowledgments
This work was supported by a Canadian Institutes of Health
Research New Investigator award and Open Operating Grant
CRN-142393, Cancer Research Society Operating Grants
CRS-22641 and CRS-24368, Natural Sciences and Engineering
Research Council of Canada Discovery Grants NSERC-201405218 and NSERC-2020-04241, and Michael Smith Foundation
for Health Research Scholar Award 17686. The authors declare no
conflicts of interest with the contents of this chapter.
References
1. Konermann L, Pan J, Liu Y-H (2011) Hydrogen exchange mass spectrometry for studying
protein structure and dynamics. Chem Soc Rev
40:1224–1234
2. Masson GR, Jenkins ML, Burke JE (2017) An
overview of hydrogen deuterium exchange
mass spectrometry (HDX-MS) in drug discovery. Expert Opin Drug Discovery 12:981–994
3. Vadas O, Jenkins ML, Dornan GL et al (2017)
Using hydrogen-deuterium exchange mass
spectrometry to examine protein-membrane
interactions. Methods Enzymol 583:143–172
4. Deng B, Lento C, Wilson DJ (2016) Hydrogen deuterium exchange mass spectrometry in
biopharmaceutical discovery and development—a review. Anal Chim Acta 940:8–20
5. Harrison RA, Engen JR (2016) Conformational insight into multi-protein signaling
assemblies by hydrogen-deuterium exchange
mass spectrometry. Curr Opin Struct Biol
41:187–193
6. Gallagher ES, Hudgens JW (2016) Mapping
protein-ligand interactions with proteolytic
fragmentation,
hydrogen/deuterium
exchange-mass spectrometry. Methods Enzymol 566:357–404
7. Guttman M, Lee KK (2016) Isotope labeling
of biomolecules: structural analysis of viruses
by HDX-MS. Methods Enzymol 566:405–426
8. Vadas O, Burke JE (2015) Probing the
dynamic regulation of peripheral membrane
proteins using hydrogen deuterium exchangeMS (HDX-MS). Biochem Soc Trans
43:773–786
9. Pirrone GF, Iacob RE, Engen JR (2014) Applications of hydrogen/deuterium exchange MS
from 2012 to 2014. Anal Chem 87(1): 99–118
10. Balasubramaniam D, Komives EA (2013)
Hydrogen-exchange mass spectrometry for
the study of intrinsic disorder in proteins. Biochim Biophys Acta 1834:1202–1209
11. Rostislavleva K, Soler N, Ohashi Y et al (2015)
Structure and flexibility of the endosomal
Vps34 complex reveals the basis of its function
on membranes. Science 350:aac7365
12. Jenkins ML, Margaria JP, Stariha JTB et al
(2018) Structural determinants of Rab11 activation by the guanine nucleotide exchange factor SH3BP5. Nat Commun 9:3772
13. Kielkopf CS, Ghosh M, Anand GS et al (2018)
HDX-MS reveals orthosteric and allosteric
changes in apolipoprotein-D structural dynamics upon binding of progesterone. Protein Sci
282:31068–31374
14. Pulkoski-Gross MJ, Jenkins ML, Truman J-P
et al (2018) An intrinsic lipid-binding interface
controls sphingosine kinase 1 function. J Lipid
Res 59:462–474
15. Luc ˇic ´ I, Rathinaswamy MK, Truebestein L et al
(2018) Conformational sampling of membranes by Akt controls its activation and inactivation. Proc Natl Acad Sci U S A 115:
E3940–E3949
16. Martens C, Shekhar M, Borysik AJ et al (2018)
Direct protein-lipid interactions shape the conformational landscape of secondary transporters. Nat Commun 9:4151
17. Adhikary S, Deredge DJ, Nagarajan A et al
(2017) Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer.
Proc Natl Acad Sci U S A 114:E1786–E1795
18. Shukla AK, Westfield GH, Xiao K et al (2014)
Visualization of arrestin recruitment by a Gprotein-coupled receptor. Nature
19. Mehmood S, Domene C, Forest E et al (2012)
Dynamics of a bacterial multidrug ABC transporter in the inward- and outward-facing conformations. Proc Natl Acad Sci U S A
109:10832–10836
20. West GM, Chien EYT, Katritch V et al (2011)
Ligand-dependent perturbation of the conformational ensemble for the GPCR β2 adrenergic
484
Jordan T. B. Stariha et al.
This work was supported by a Canadian Institutes of Health
Research New Investigator award and Open Operating Grant
CRN-142393, Cancer Research Society Operating Grants
CRS-22641 and CRS-24368, Natural Sciences and Engineering
Research Council of Canada Discovery Grants NSERC-201405218 and NSERC-2020-04241, and Michael Smith Foundation
for Health Research Scholar Award 17686. The authors declare no
conflicts of interest with the contents of this chapter.
References
1. Konermann L, Pan J, Liu Y-H (2011) Hydrogen exchange mass spectrometry for studying
protein structure and dynamics. Chem Soc Rev
40:1224–1234
2. Masson GR, Jenkins ML, Burke JE (2017) An
overview of hydrogen deuterium exchange
mass spectrometry (HDX-MS) in drug discovery. Expert Opin Drug Discovery 12:981–994
3. Vadas O, Jenkins ML, Dornan GL et al (2017)
Using hydrogen-deuterium exchange mass
spectrometry to examine protein-membrane
interactions. Methods Enzymol 583:143–172
4. Deng B, Lento C, Wilson DJ (2016) Hydrogen deuterium exchange mass spectrometry in
biopharmaceutical discovery and development—a review. Anal Chim Acta 940:8–20
5. Harrison RA, Engen JR (2016) Conformational insight into multi-protein signaling
assemblies by hydrogen-deuterium exchange
mass spectrometry. Curr Opin Struct Biol
41:187–193
6. Gallagher ES, Hudgens JW (2016) Mapping
protein-ligand interactions with proteolytic
fragmentation,
hydrogen/deuterium
exchange-mass spectrometry. Methods Enzymol 566:357–404
7. Guttman M, Lee KK (2016) Isotope labeling
of biomolecules: structural analysis of viruses
by HDX-MS. Methods Enzymol 566:405–426
8. Vadas O, Burke JE (2015) Probing the
dynamic regulation of peripheral membrane
proteins using hydrogen deuterium exchangeMS (HDX-MS). Biochem Soc Trans
43:773–786
9. Pirrone GF, Iacob RE, Engen JR (2014) Applications of hydrogen/deuterium exchange MS
from 2012 to 2014. Anal Chem 87(1): 99–118
10. Balasubramaniam D, Komives EA (2013)
Hydrogen-exchange mass spectrometry for
the study of intrinsic disorder in proteins. Biochim Biophys Acta 1834:1202–1209
11. Rostislavleva K, Soler N, Ohashi Y et al (2015)
Structure and flexibility of the endosomal
Vps34 complex reveals the basis of its function
on membranes. Science 350:aac7365
12. Jenkins ML, Margaria JP, Stariha JTB et al
(2018) Structural determinants of Rab11 activation by the guanine nucleotide exchange factor SH3BP5. Nat Commun 9:3772
13. Kielkopf CS, Ghosh M, Anand GS et al (2018)
HDX-MS reveals orthosteric and allosteric
changes in apolipoprotein-D structural dynamics upon binding of progesterone. Protein Sci
282:31068–31374
14. Pulkoski-Gross MJ, Jenkins ML, Truman J-P
et al (2018) An intrinsic lipid-binding interface
controls sphingosine kinase 1 function. J Lipid
Res 59:462–474
15. Luc ˇic ´ I, Rathinaswamy MK, Truebestein L et al
(2018) Conformational sampling of membranes by Akt controls its activation and inactivation. Proc Natl Acad Sci U S A 115:
E3940–E3949
16. Martens C, Shekhar M, Borysik AJ et al (2018)
Direct protein-lipid interactions shape the conformational landscape of secondary transporters. Nat Commun 9:4151
17. Adhikary S, Deredge DJ, Nagarajan A et al
(2017) Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer.
Proc Natl Acad Sci U S A 114:E1786–E1795
18. Shukla AK, Westfield GH, Xiao K et al (2014)
Visualization of arrestin recruitment by a Gprotein-coupled receptor. Nature
19. Mehmood S, Domene C, Forest E et al (2012)
Dynamics of a bacterial multidrug ABC transporter in the inward- and outward-facing conformations. Proc Natl Acad Sci U S A
109:10832–10836
20. West GM, Chien EYT, Katritch V et al (2011)
Ligand-dependent perturbation of the conformational ensemble for the GPCR β2 adrenergic
484
Jordan T. B. Stariha et al.