Hydrogen Exchange: the Modern Legacy of Linderstrøm-Lang

Overview

Journal Protein Sci

Specialty Biochemistry

Date 1997 May 1

PMID 9144782

Citations 94

Authors

S W Englander

L Mayne

Y Bai

T R Sosnick

Affiliations

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Abstract

This discussion, prepared for the Protein Society's symposium honoring the 100th anniversary of Kaj Linderstrøm-Lang, shows how hydrogen exchange approaches initially conceived and implemented by Lang and his colleagues some 50 years ago are contributing to current progress in structural biology. Examples are chosen from the active protein folding field. Hydrogen exchange methods now make it possible to define the structure of protein folding intermediates in various contexts: as tenuous molten globule forms at equilibrium under destabilizing conditions, in kinetic intermediates that exist for less than one second, and as infinitesimally populated excited state forms under native conditions. More generally, similar methods now find broad application in studies of protein structure, energetics, and interactions. This article considers the rise of these capabilities from their inception at the Carlsberg Labs to their contemporary role as a significant tool of modern structural biology.

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References

Chamberlain A, Handel T, Marqusee S . Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nat Struct Biol. 1996; 3(9):782-7. DOI: 10.1038/nsb0996-782. View

Rodgers M, Englander J, Englander S, Harrington W . Measurement of protein structure change in active muscle by hydrogen-tritium exchange. Biophys Chem. 1996; 59(3):221-30. DOI: 10.1016/0301-4622(95)00133-6. View

Bai Y, Englander S . Future directions in folding: the multi-state nature of protein structure. Proteins. 1996; 24(2):145-51. DOI: 10.1002/(SICI)1097-0134(199602)24:2<145::AID-PROT1>3.0.CO;2-I. View

Raschke T, Marqusee S . The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nat Struct Biol. 1997; 4(4):298-304. DOI: 10.1038/nsb0497-298. View

HVIDT A, LinderstrOm-Lang K . Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions. Biochim Biophys Acta. 1954; 14(4):574-5. DOI: 10.1016/0006-3002(54)90241-3. View

Berger A, LinderstrOm-Lang K . Deuterium exchange of poly-DL-alanine in aqueous solution. Arch Biochem Biophys. 1957; 69:106-18. DOI: 10.1016/0003-9861(57)90478-2. View

KRAUSE I, LINDSTROM-LANG K . Exchange of deuterium and 18O between water and other substances. II. Alternative-methods. C R Trav Lab Carlsberg Chim. 1955; 29(22-23):367-84. View

Benson E, LinderstrOm-Lang K . Deuterium exchange between myoglobin and water. Biochim Biophys Acta. 1959; 32:579-81. DOI: 10.1016/0006-3002(59)90649-3. View

HVIDT A, Nielsen S . Hydrogen exchange in proteins. Adv Protein Chem. 1966; 21:287-386. DOI: 10.1016/s0065-3233(08)60129-1. View

10.

Tsuboi M, Nakanishi M . Overall and localized fluctuation in the structure of a protein molecule. Adv Biophys. 1979; 12:101-30. View

11.

ROSA J, Richards F . An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: application to ribonuclease S peptide. J Mol Biol. 1979; 133(3):399-416. DOI: 10.1016/0022-2836(79)90400-5. View

12.

Barksdale A, Rosenberg A . Acquisition and interpretation of hydrogen exchange data from peptides, polymers, and proteins. Methods Biochem Anal. 1982; 28:1-113. DOI: 10.1002/9780470110485.ch1. View

13.

Kim P, Baldwin R . Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Biochem. 1982; 51:459-89. DOI: 10.1146/annurev.bi.51.070182.002331. View

14.

Wagner G, Wuthrich K . Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance. J Mol Biol. 1982; 160(2):343-61. DOI: 10.1016/0022-2836(82)90180-2. View

15.

Woodward C, Simon I, Tuchsen E . Hydrogen exchange and the dynamic structure of proteins. Mol Cell Biochem. 1982; 48(3):135-60. DOI: 10.1007/BF00421225. View

16.

Englander J, Rogero J, Englander S . Protein hydrogen exchange studied by the fragment separation method. Anal Biochem. 1985; 147(1):234-44. PMC: 3442362. DOI: 10.1016/0003-2697(85)90033-8. View

17.

Pace C . Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 1986; 131:266-80. DOI: 10.1016/0076-6879(86)31045-0. View

18.

Rogero J, Englander J, Englander S . Individual breathing reactions measured by functional labeling and hydrogen exchange methods. Methods Enzymol. 1986; 131:508-17. DOI: 10.1016/0076-6879(86)31053-x. View

19.

SCHELLMAN J . Selective binding and solvent denaturation. Biopolymers. 1987; 26(4):549-59. DOI: 10.1002/bip.360260408. View

20.

Udgaonkar J, Baldwin R . NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature. 1988; 335(6192):694-9. DOI: 10.1038/335694a0. View