Literature DB >> 313338

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.

G Wagner, A J Kalb, K Wüthrich.   

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Year:  1979        PMID： 313338     DOI： 10.1111/j.1432-1033.1979.tb12960.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


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  3 in total

1.  Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor.

Authors:  Linda Foit; Antje Mueller-Schickert; Bharath S Mamathambika; Stefan Gleiter; Caitlyn L Klaska; Guoping Ren; James C A Bardwell
Journal:  Antioxid Redox Signal       Date:  2011-01-23       Impact factor: 8.401

2.  Correlations between internal mobility and stability of globular proteins.

Authors:  K Wüthrich; G Wagner; R Richarz; W Braun
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

3.  Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues.

Authors:  K Uchida; Y Miyake; M Kainosho
Journal:  J Biomol NMR       Date:  1991-05       Impact factor: 2.835
  3 in total

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