Literature DB >> 22911160

(1)H, (13)C and (15)N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus.

R H Fogh1, D Schipper, R Boelens, R Kaptein.   

Abstract

The (1)H, (13)C and (15)N NMR resonances of the backbone of serine protease PB92 have been assigned. This 269-residue protein is one of the largest monomeric proteins assigned so far. The amount and quality of information available suggest that even larger proteins could be assigned with present methods. Measured chemical shifts show excellent agreement with the secondary structure.

Entities:  

Year:  1994        PMID： 22911160     DOI： 10.1007/BF00178340

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN： 0925-2738            Impact factor:   2.835


  13 in total

1.  Crystal structure of the high-alkaline serine protease PB92 from Bacillus alcalophilus.

Authors:  J M van der Laan; A V Teplyakov; H Kelders; K H Kalk; O Misset; L J Mulleners; B W Dijkstra
Journal:  Protein Eng       Date:  1992-07

Review 2.  Protein engineering. The design, synthesis and characterization of factitious proteins.

Authors:  W V Shaw
Journal:  Biochem J       Date:  1987-08-15       Impact factor: 3.857

Review 3.  Prospects for NMR of large proteins.

Authors:  G Wagner
Journal:  J Biomol NMR       Date:  1993-07       Impact factor: 2.835

4.  Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta.

Authors:  D Marion; P C Driscoll; L E Kay; P T Wingfield; A Bax; A M Gronenborn; G M Clore
Journal:  Biochemistry       Date:  1989-07-25       Impact factor: 3.162

5.  1H, 13C, and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycin.

Authors:  R X Xu; D Nettesheim; E T Olejniczak; R Meadows; G Gemmecker; S W Fesik
Journal:  Biopolymers       Date:  1993-04       Impact factor: 2.505

6.  1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma.

Authors:  S Grzesiek; H Döbeli; R Gentz; G Garotta; A M Labhardt; A Bax
Journal:  Biochemistry       Date:  1992-09-08       Impact factor: 3.162

7.  P NMR and mass spectrometry of atropinesterase and some serine proteases phosphorylated with a transition-state analogue.

Authors:  A C van der Drift; H C Beck; W H Dekker; A G Hulst; E R Wils
Journal:  Biochemistry       Date:  1985-11-19       Impact factor: 3.162

8.  Complete assignments of magnetic resonances of ribonuclease H from Escherichia coli by double- and triple-resonance 2D and 3D NMR spectroscopies.

Authors:  T Yamazaki; M Yoshida; K Nagayama
Journal:  Biochemistry       Date:  1993-06-01       Impact factor: 3.162

9.  Protein engineering of the high-alkaline serine protease PB92 from Bacillus alcalophilus: functional and structural consequences of mutation at the S4 substrate binding pocket.

Authors:  A V Teplyakov; J M van der Laan; A A Lammers; H Kelders; K H Kalk; O Misset; L J Mulleners; B W Dijkstra
Journal:  Protein Eng       Date:  1992-07

10.  Relationship between nuclear magnetic resonance chemical shift and protein secondary structure.

Authors:  D S Wishart; B D Sykes; F M Richards
Journal:  J Mol Biol       Date:  1991-11-20       Impact factor: 5.469
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  7 in total

1.  Expression of human chorionic gonadotropin uniformly labeled with NMR isotopes in Chinese hamster ovary cells: an advance toward rapid determination of glycoprotein structures.

Authors:  J W Lustbader; S Birken; S Pollak; A Pound; B T Chait; U A Mirza; S Ramnarain; R E Canfield; J M Brown
Journal:  J Biomol NMR       Date:  1996-06       Impact factor: 2.835

2.  Resonance assignments for Oncostatin M, a 24-kDa alpha-helical protein.

Authors:  R C Hoffman; F J Moy; V Price; J Richardson; D Kaubisch; E A Frieden; J D Krakover; B J Castner; J King; C J March; R Powers
Journal:  J Biomol NMR       Date:  1996-06       Impact factor: 2.835

3.  Secondary structure of beta-hydroxydecanoyl thiol ester dehydrase, a 39-kDa protein, derived from H alpha, C alpha, C beta and CO signal assignments and the Chemical Shift Index: comparison with the crystal structure.

Authors:  V Copié; J A Battles; J M Schwab; D A Torchia
Journal:  J Biomol NMR       Date:  1996-06       Impact factor: 2.835

4.  Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.

Authors:  I Sethson; U Edlund; T A Holak; A Ross; B H Jonsson
Journal:  J Biomol NMR       Date:  1996-12       Impact factor: 2.835

5.  High-level 2H/13C/15N labeling of proteins for NMR studies.

Authors:  R A Venters; C C Huang; B T Farmer; R Trolard; L D Spicer; C A Fierke
Journal:  J Biomol NMR       Date:  1995-06       Impact factor: 2.835

6.  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

Review 7.  The blind watchmaker and rational protein engineering.

Authors:  H W Anthonsen; A Baptista; F Drabløs; P Martel; S B Petersen
Journal:  J Biotechnol       Date:  1994-08-31       Impact factor: 3.307
  7 in total

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