Pages that link to "Q40715069"
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The following pages link to Conformational Studies by 1H Nuclear Magnetic Resonance of the Basic Pancreatic Trypsin Inhibitor after Reduction of the Disulfide Bond between Cys-14 and Cys-38. Influence of Charged Protecting Groups on the Stability of the Protein (Q40715069):
Displaying 15 items.
- Correlations between internal mobility and stability of globular proteins (Q34251694) (← links)
- Two-dimensional 1H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor. Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein (Q36592926) (← links)
- The Influence of Localized Chemical Modifications of the Basic Pancreatic Trypsin Inhibitor on Static and Dynamic Aspects of the Molecular Conformation in Solution (Q40715062) (← links)
- Genetic Selection for Enhanced FoldingIn VivoTargets the Cys14-Cys38 Disulfide Bond in Bovine Pancreatic Trypsin Inhibitor (Q42627750) (← links)
- Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins (Q43898083) (← links)
- Structural Characterization by Nuclear Magnetic Resonance of a Reactive-Site 13Carbon-labelled Basic Pancreatic Trypsin Inhibitor with the Peptide Bond Arg-39-Ala-40 Cleaved and Arg-39 Removed (Q44179483) (← links)
- Insight into the stability of the hydrophobic binding proteins ofescherichia coli:Assessing the proteins for use as biosensors (Q44601566) (← links)
- Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. (Q52708432) (← links)
- Reductive cleavage and regeneration of the disulfide bonds inStreptomyces subtilisin inhibitor (SSI) as studied by the carbonyl13C NMR resonances of cysteinyl residues (Q67908757) (← links)
- Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 1. Combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labil (Q72631460) (← links)
- Role of the environment in the refolding of reduced pancreatic trypsin inhibitor (Q72639390) (← links)
- Evolutionary conservation and variation of protein folding pathways. Two protease inhibitor homologues from black mamba venom (Q72709867) (← links)
- Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor (Q72750352) (← links)
- Folding pathway of a circular form of bovine pancreatic trypsin inhibitor (Q72753385) (← links)
- p2H dependence of the exchange with the solvent of interior amide protons in basic pancreatic trypsin inhibitor modified by reduction of the disulfide bond 1438 (Q72899359) (← links)