Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. - Wikidata - awgldk - TriplyDB

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

http://www.wikidata.org/entity/Q36199183

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Protein folding: then and now Identification of compact, hydrophobically stabilized domains and modules containing multiple peptide chains Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation The nature of protein folding pathways Using deeply trapped intermediates to map the cytochrome c folding landscape A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy Is an intermediate state populated on the folding pathway of ubiquitin?From Levinthal to pathways to funnels Quarternary structure amplification of protein folding differences observed in 'native' platelet factor-4 Observation of the closing of individual hydrogen bonds during TFE-induced helix formation in a peptide Structural transformations of cytochrome c upon interaction with cardiolipin Start2Fold: a database of hydrogen/deuterium exchange data on protein folding and stability Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor Nonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methods Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods.Identification of rare partially unfolded states in equilibrium with the native conformation in an all beta-barrel protein.Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange Structural events during the refolding of an all beta-sheet protein.Mechanism of protein folding.A fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange protection factors in the range reported for "molten globules".Reversible unfolding and refolding behavior of a monomeric aldolase from Staphylococcus aureus Tracking lysozyme unfolding during salt-induced precipitation with hydrogen exchange and mass spectrometry.Structural features of interferon-gamma aggregation revealed by hydrogen exchange.Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.Inter- and intra-molecular migration of peptide amide hydrogens during electrospray ionization.A lattice model for protein structure prediction at low resolution Protein folding and misfolding: mechanism and principles.NMR studies of mobility within protein structure.Directionality in protein fold prediction.HDX-analyzer: a novel package for statistical analysis of protein structure dynamics Principles of protein folding--a perspective from simple exact models.Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c Autonomous subdomains in protein folding.Comparison of kinetics of formation of helices and hydrophobic core during the folding of staphylococcal nuclease from acid Origins of structural diversity within sequentially identical hexapeptides.Mechanisms and uses of hydrogen exchange.Future directions in folding: the multi-state nature of protein structure.Hydrogen exchange: the modern legacy of Linderstrøm-Lang.NMR and CD conformational studies of the C-terminal 16-peptides of Pseudomonas aeruginosa c551 and Hydrogenobacter thermophilus c552 cytochromes.Structural characterization of protein kinase A as a function of nucleotide binding. Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection.

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Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

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P2860

Hydrogen exchange and structural dynamics of proteins and nucleic acids

Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons.

Is there a single pathway for the folding of a polypeptide chain?

Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.

Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group.

Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange.

Experimental studies of protein folding and unfolding.

Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding.

Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues.

A model of myoglobin self-organization.

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