Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus.

Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus.

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http://www.wikidata.org/entity/Q30830434

Q30830434

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Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein Relative stabilities of conserved and non-conserved structures in the OB-fold superfamily.Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.Type 1 and Type 2 scenarios in hydrogen exchange mass spectrometry studies on protein-ligand complexes.CLIPS-1D: analysis of multiple sequence alignments to deduce for residue-positions a role in catalysis, ligand-binding, or protein structure Clusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability.Betaalpha-hairpin clamps brace betaalphabeta modules and can make substantive contributions to the stability of TIM barrel proteins.Protein dynamics governed by interfaces of high polarity and low packing density.Design of symmetric TIM barrel proteins from first principles.NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein.Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Repeat-protein folding: new insights into origins of cooperativity, stability, and topology.Steroid and protein ligand binding to cytochrome P450 46A1 as assessed by hydrogen-deuterium exchange and mass spectrometry.Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate state What lessons can be learned from studying the folding of homologous proteins?Folding of proteins with a flavodoxin-like architecture.Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.The foldon substructure of staphylococcal nuclease Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Gō model simulation.The folding pathway of glycosomal triosephosphate isomerase: structural insights into equilibrium intermediates.Roles for the two N-terminal (β/α) modules in the folding of a (β/α)₈-barrel protein as studied by fragmentation analysis.

P2860

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P2860

Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus.

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http://www.wikidata.org/entity/Q30830434

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2007 nî lūn-bûn

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2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2007年の論文

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