Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways

scientific article published on November 1993

Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode1993PNAS...90.9837C
P356DOI10.1073/PNAS.90.21.9837
P932PMC publication ID47667
P698PubMed publication ID8234322
P5875ResearchGate publication ID14965612

P50authorAlan FershtQ537479
P2093author name stringClarke J
Bycroft M
Hounslow AM
P2860cites workHydrogen exchange in thermally denatured ribonuclease A.Q46110989
Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes.Q52708432
Primary structure effects on peptide group hydrogen exchange.Q52994305
Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.Q54151191
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 proteinQ57564237
A nuclear magnetic resonance study of the hydrogen-exchange behaviour of lysozyme in crystals and solutionQ57889980
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 studiesQ68101605
The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical modelsQ68101608
Correlation of hydrogen exchange behaviour and thermal stability of lysozymeQ71833723
Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonanceQ72684541
Tissue sulfhydryl groupsQ26778486
Hydrogen exchange and structural dynamics of proteins and nucleic acidsQ28262950
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein foldingQ28306201
The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedureQ28306221
The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedureQ28306230
Stable submolecular folding units in a non-compact form of cytochrome cQ30353627
Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitorQ30686884
Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solutionQ30847689
Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitorQ34251701
Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturationQ34363628
Protein folding studied using hydrogen-exchange labeling and two-dimensional NMRQ35836954
Molecular structure of a new family of ribonucleasesQ36646102
Hydrogen Exchange in ProteinsQ40040717
Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitorQ41745237
Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR studyQ41861339
Hydrogen exchange in native and denatured states of hen egg-white lysozymeQ44184711
P433issue21
P407language of work or nameEnglishQ1860
P921main subjectprotein foldingQ847556
P304page(s)9837-9841
P577publication date1993-11-01
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleLocal breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways
P478volume90

Reverse relations

cites work (P2860)
Q35835636A kinetically significant intermediate in the folding of barnase
Q30326441Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.
Q30426755An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway
Q43600485Differences in the pathways for unfolding and hydrogen exchange among mutants of Escherichia coli alkaline phosphatase
Q77221322Evidence for an unfolding and refolding pathway in cytochrome c
Q48674028Flexibility of the murine prion protein and its Asp178Asn mutant investigated by molecular dynamics simulations.
Q30981774How amide hydrogens exchange in native proteins
Q34461691Hydrogen exchange and protein folding.
Q30416869Hydrogen exchange in BPTI variants that do not share a common disulfide bond
Q30429846Hydrogen exchange studies of protein structure
Q46776717Induction of flexibility through protein-protein interactions
Q93031304Measurement of Very Fast Exchange Rates of Individual Amide Protons in Proteins by NMR Spectroscopy
Q38810874Protein dynamics and function from solution state NMR spectroscopy
Q30322816Residue depth: a novel parameter for the analysis of protein structure and stability.
Q41679938Structural and mechanistic consequences of polypeptide binding by GroEL.
Q34811742Studies of biomolecular conformations and conformational dynamics by mass spectrometry
Q36281825The effects of disulfide bonds on the denatured state of barnase
Q43028082Thermodynamic and kinetic stability of a large multi-domain enzyme from the hyperthermophile Aeropyrum pernix
Q41566813Touring the landscapes: partially folded proteins examined by hydrogen exchange
Q37229567beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

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