Pages that link to "Q45845527"

The following pages link to Escherichia coli thioredoxin folds into two compact forms of different stability to urea denaturation (Q45845527):

Displaying 24 items.

• Crystal structure of human micro-crystallin complexed with NADPH (Q24294217) (← links)
• Reactivity of Thioredoxin as a Protein Thiol-Disulfide Oxidoreductase (Q24630110) (← links)
• The conformational stability and biophysical properties of the eukaryotic thioredoxins of Pisum sativum are not family-conserved (Q28477238) (← links)
• The malaria parasite Plasmodium falciparum possesses a functional thioredoxin system (Q32062534) (← links)
• 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin (Q34115506) (← links)
• Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy (Q35479250) (← links)
• Mutation of conserved residues in Escherichia coli thioredoxin: Effects on stability and function (Q36277627) (← links)
• Unnatural amino acid packing mutants of Escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques (Q36278018) (← links)
• Coupling between trans/cis proline isomerization and protein stability in staphylococcal nuclease (Q36280126) (← links)
• NMR analysis of cleaved Escherichia coli thioredoxin (1-73/74-108) and its P76A variant: cis/trans peptide isomerization (Q36281708) (← links)
• Solid-state NMR spectroscopy of protein complexes (Q36961610) (← links)
• Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein (Q37630885) (← links)
• Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions. (Q38634845) (← links)
• Secondary-structure analysis of denatured proteins by vacuum-ultraviolet circular dichroism spectroscopy (Q42112486) (← links)
• Interaction with magnesium and ADP stabilizes both components of nitrogenase from Klebsiella pneumoniae against urea denaturation (Q42847273) (← links)
• Reduced spectral density mapping of a partially folded fragment of E. coli thioredoxin (Q47213146) (← links)
• Recognition between a short unstructured peptide and a partially folded fragment leads to the thioredoxin fold sharing native-like dynamics. (Q54341270) (← links)
• Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin. (Q54634397) (← links)
• Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein. (Q54640373) (← links)
• Improved synthetic methods for the selective deuteration of aromatic amino acids: applications of selective protonation towards the identification of protein folding intermediates through nuclear magnetic resonance. (Q54655748) (← links)
• The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability (Q54694210) (← links)
• Heat capacity analysis of oxidized Escherichia coli thioredoxin fragments (1--73, 74--108) and their noncovalent complex. Evidence for the burial of apolar surface in protein unfolded states (Q73569219) (← links)
• A single dipeptide sequence modulates the redox properties of a whole enzyme family (Q74486160) (← links)
• Redox control of hydrogenase activity in the green alga Scenedesmus obliquus by thioredoxin and other thiols (Q78068347) (← links)