Literature DB >> 1540633

H-NMR studies of native and fragmented subtilisin Carlsberg.

R Consonni1, H Molinari, F Greco, G Zannoni, L Zetta, G Carrea, S Riva.   

Abstract

NMR studies have been carried out on subtilisin Carlsberg in order to identify the sharp resonances observed in the proton spectra of the enzyme dissolved in aqueous solution. NMR spectra, obtained with the combination of spin-echo and selective excitation sequences, from both the native and inactivated protein, enabled us to assign sharp signals to subtilisin fragments derived from enzymatic autolysis (monitored by high-performance size-exclusion chromatography), rather than to mobile segments of the intact protein.

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Year:  1992        PMID: 1540633     DOI: 10.1016/0167-4838(92)90231-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Unusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis.

Authors:  E L Ash; J L Sudmeier; R M Day; M Vincent; E V Torchilin; K C Haddad; E M Bradshaw; D G Sanford; W W Bachovchin
Journal:  Proc Natl Acad Sci U S A       Date:  2000-09-12       Impact factor: 11.205

2.  Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMR.

Authors:  Regina M Day; Craig J Thalhauser; James L Sudmeier; Matthew P Vincent; Ekaterina V Torchilin; David G Sanford; Christopher W Bachovchin; William W Bachovchin
Journal:  Protein Sci       Date:  2003-04       Impact factor: 6.725

3.  Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus.

Authors:  R H Fogh; D Schipper; R Boelens; R Kaptein
Journal:  J Biomol NMR       Date:  1995-04       Impact factor: 2.835

  3 in total

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