DOI: 10.1016/s1359-0278(96)00038-7. An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway

An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway

10.1016/s1359-0278(96)00038-7

Crossref journal-article

Elsevier BV

Folding and Design (78)

Bibliography

Clarke, J., & Fersht, A. R. (1996). An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Folding and Design, 1(4), 243â254.

Authors 2

Jane Clarke (first)
Alan R Fersht (additional)

References 37 Referenced 86

10.1016/0022-2836(82)90180-2 / J. Mol. Biol / Amide proton exchange and surface conformation of BPTI in solution by Wagner (1982)
10.1017/S0033583500005217 / Quart. Rev. Biophys / Hydrogen exchange and structural dynamics of proteins and nucleic acids by Englander (1984)
10.1016/0022-2836(91)90722-I / J. Mol. Biol / A NMR study of the hydrogen-exchange behaviour of lysozyme in crystals and solution by Pedersen (1991)
10.1021/bi00134a020 / Biochemistry / Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution by Gallagher (1992)
10.1002/prot.340140210 / Proteins / Hydrogen exchange in native and denatured states of hen egg white lysozyme by Radford (1992)
10.1021/bi00088a012 / Biochemistry / Hydrogen exchange identifies native state motional domains important in protein folding by Kim (1993)
10.1016/S0065-3233(08)60129-1 / Adv. Protein Chem / Hydrogen exchange in proteins by Hvidt (1966)
10.1146/annurev.bb.08.060179.000531 / Annu. Rev. Biophys. Bioeng / Hydrogen exchange kinetics and internal motions in proteins and nucleic acids by Woodward (1979)
10.1021/bi00346a055 / Biochemistry / Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic inhibitor at variable p2H and temperature by Roder (1985)
10.1016/0022-2836(91)80191-V / J. Mol. Biol / Stable submolecular folding units in a non-compact form of cytochrome c by Jeng (1991)
{'key': '10.1016/S1359-0278(96)00038-7_bib11', 'first-page': '1', 'article-title': 'Deuterium exchange between peptides and water', 'volume': '2', 'author': 'Linderstrøm-Lang', 'year': '1955', 'journal-title': 'Chem Soc. (London), Spec. Publ'} / Chem Soc. (London), Spec. Publ / Deuterium exchange between peptides and water by Linderstrøm-Lang (1955)
10.1126/science.8235609 / Science / Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A by Mayo (1993)
10.1126/science.7618079 / Science / Protein folding intermediates: native state hydrogen exchange by Bai (1995)
10.1016/S0065-3233(08)60241-7 / Adv. Protein Chem / Protein folding. Part C by Tanford (1970)
10.1002/prot.340200103 / Proteins / Protein stability parameters measured by hydrogen exchange by Bai (1994)
10.1073/pnas.90.21.9837 / Proc. Natl. Acad. Sci. USA / Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways by Clarke (1993)
10.1021/bi00029a003 / Biochemistry / The relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase by Perrett (1995)
10.1016/0022-2836(92)90564-Z / J. Mol. Biol / The folding of an enzyme IV. Structure of the intermediate in the refolding of barnase analysed by a protein engineering procedure by Matouschek (1992)
10.1021/bi00193a001 / Biochemistry / Protein hydrogen exchange in denaturant: quantitative analysis by a two-process model by Qian (1994)
10.1016/S0022-2836(83)80309-X / J. Mol. Biol / Correlation of hydrogen exchange behaviour and thermal stability of lysozyme by Delepierre (1983)
10.1021/bi00346a056 / Biochemistry / Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor by Roder (1985)
10.1021/bi00088a013 / Biochemistry / Protein internal flexibility and global stability: effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor by Kim (1993)
10.1073/pnas.93.5.1982 / Proc. Natl. Acad. Sci. USA / A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions by Loh (1996)
10.1002/prot.340170110 / Proteins / Primary structure effects on peptide group hydrogen exchange by Bai (1993)
10.1021/bi00067a022 / Biochemistry / Engineering disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation by Clarke (1993)
10.1021/bi00752a003 / Biochemistry / Primary structure effects on peptide group hydrogen exchange by Molday (1972)
10.1126/science.8235611 / Science / Detection of transient protein folding populations by mass spectrometry by Miranker (1993)
10.1016/0022-2836(92)90524-N / J. Mol. Biol / Nuclear magnetic resonance studies of the internal dynamics in Apo, (Cd2+)1 and (Ca2+)2 calbindin D9k. The rates of amide proton exchange with solvent by Skelton (1992)
10.1002/prot.340170111 / Proteins / Isotope effect in peptide group hydrogen exchange by Connelly (1993)
10.1073/pnas.91.20.9412 / Proc. Natl. Acad. Sci. USA / Towards solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state by Arcus (1994)
10.1002/pro.5560040921 / Protein Sci / A statistical mechanical model for hydrogen exchange in globular proteins by Miller (1995)
10.1021/bi00111a022 / Biochemistry / Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR by Meiering (1991)
10.1016/0968-0004(93)90086-3 / Trends Biochem. Sci / Is the slow-exchange core the protein folding core? by Woodward (1993)
10.1016/S0959-440X(94)90068-X / Curr. Opin. Struct. Biol / Hydrogen exchange rates and protein folding by Woodward (1994)
10.1021/j100830a521 / J. Phys. Chem / Use of a glass electrode to measure acidities in deuterium oxide by Glasoe (1960)
{'key': '10.1016/S1359-0278(96)00038-7_bib36', 'first-page': '304', 'article-title': 'Comparison of different modes of 2-dimensional reverse correlation NMR for the study of proteins', 'volume': '86', 'author': 'Bax', 'year': '1990', 'journal-title': 'J. Magn. Reson'} / J. Magn. Reson / Comparison of different modes of 2-dimensional reverse correlation NMR for the study of proteins by Bax (1990)
10.1038/297162a0 / Nature / Molecular structure of a new family of ribonucleases by Mauguen (1982)

Dates

Type	When
Created	20 years, 1 month ago (July 7, 2005, 11:24 a.m.)
Deposited	6 years, 7 months ago (Jan. 24, 2019, 12:51 p.m.)
Indexed	1 year, 5 months ago (March 4, 2024, 5:02 p.m.)
Issued	29 years, 1 month ago (Aug. 1, 1996)
Published	29 years, 1 month ago (Aug. 1, 1996)
Published Print	29 years, 1 month ago (Aug. 1, 1996)

Funders 0

None

BibTeX

@article{Clarke_1996, title={An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway}, volume={1}, ISSN={1359-0278}, url={http://dx.doi.org/10.1016/s1359-0278(96)00038-7}, DOI={10.1016/s1359-0278(96)00038-7}, number={4}, journal={Folding and Design}, publisher={Elsevier BV}, author={Clarke, Jane and Fersht, Alan R}, year={1996}, month=aug, pages={243–254} }

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