scholarly article | Q13442814 |
P819 | ADS bibcode | 1993PNAS...90.9837C |
P356 | DOI | 10.1073/PNAS.90.21.9837 |
P932 | PMC publication ID | 47667 |
P698 | PubMed publication ID | 8234322 |
P5875 | ResearchGate publication ID | 14965612 |
P50 | author | Alan Fersht | Q537479 |
P2093 | author name string | Clarke J | |
Bycroft M | |||
Hounslow AM | |||
P2860 | cites work | Hydrogen exchange in thermally denatured ribonuclease A. | Q46110989 |
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Primary structure effects on peptide group hydrogen exchange. | Q52994305 | ||
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Sequential assignment of the 1H nuclear magnetic resonance spectrum of barnase. | Q54710057 | ||
Role of arginine 67 in the stabilization of chymotrypsin inhibitor 2: examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein | Q57564237 | ||
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The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies | Q68101605 | ||
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Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance | Q72684541 | ||
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Hydrogen exchange and structural dynamics of proteins and nucleic acids | Q28262950 | ||
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The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure | Q28306221 | ||
The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure | Q28306230 | ||
Stable submolecular folding units in a non-compact form of cytochrome c | Q30353627 | ||
Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor | Q30686884 | ||
Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution | Q30847689 | ||
Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor | Q34251701 | ||
Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation | Q34363628 | ||
Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR | Q35836954 | ||
Molecular structure of a new family of ribonucleases | Q36646102 | ||
Hydrogen Exchange in Proteins | Q40040717 | ||
Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor | Q41745237 | ||
Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study | Q41861339 | ||
Hydrogen exchange in native and denatured states of hen egg-white lysozyme | Q44184711 | ||
P433 | issue | 21 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | protein folding | Q847556 |
P304 | page(s) | 9837-9841 | |
P577 | publication date | 1993-11-01 | |
P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
P1476 | title | Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways | |
P478 | volume | 90 |
Q35835636 | A kinetically significant intermediate in the folding of barnase |
Q30326441 | Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. |
Q30426755 | An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway |
Q43600485 | Differences in the pathways for unfolding and hydrogen exchange among mutants of Escherichia coli alkaline phosphatase |
Q77221322 | Evidence for an unfolding and refolding pathway in cytochrome c |
Q48674028 | Flexibility of the murine prion protein and its Asp178Asn mutant investigated by molecular dynamics simulations. |
Q30981774 | How amide hydrogens exchange in native proteins |
Q34461691 | Hydrogen exchange and protein folding. |
Q30416869 | Hydrogen exchange in BPTI variants that do not share a common disulfide bond |
Q30429846 | Hydrogen exchange studies of protein structure |
Q46776717 | Induction of flexibility through protein-protein interactions |
Q93031304 | Measurement of Very Fast Exchange Rates of Individual Amide Protons in Proteins by NMR Spectroscopy |
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Q41566813 | Touring the landscapes: partially folded proteins examined by hydrogen exchange |
Q37229567 | beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange |
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