Literature DB >> 8219743

NMR chemical shifts and structure refinement in proteins.

D D Laws1, A C de Dios, E Oldfield.   

Abstract

Computation of the 13C alpha chemical shifts (or shieldings) of glycine, alanine and valine residues in bovine and Drosophila calmodulins and Staphylococcal nuclease, and comparison with experimental values, is reported using a gauge-including atomic orbital quantum-chemical approach. The full approximately 24 ppm shielding range is reproduced (overall r.m.s.d. = 1.4 ppm) using 'optimized' protein structures, corrected for bond-length/bond-angle errors, and rovibrational effects.

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Year:  1993        PMID： 8219743     DOI： 10.1007/bf00174614

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


  13 in total

1.  Three-dimensional NMR spectroscopy of a protein in solution.

Authors:  H Oschkinat; C Griesinger; P J Kraulis; O W Sørensen; R R Ernst; A M Gronenborn; G M Clore
Journal:  Nature       Date:  1988-03-24       Impact factor: 49.962

2.  The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+, and the inhibitor pdTp, refined at 1.65 A.

Authors:  P J Loll; E E Lattman
Journal:  Proteins       Date:  1989

Review 3.  Two-dimensional NMR and protein structure.

Authors:  A Bax
Journal:  Annu Rev Biochem       Date:  1989       Impact factor: 23.643

4.  Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution.

Authors:  D A Taylor; J S Sack; J F Maune; K Beckingham; F A Quiocho
Journal:  J Biol Chem       Date:  1991-11-15       Impact factor: 5.157

5.  Calmodulin structure refined at 1.7 A resolution.

Authors:  R Chattopadhyaya; W E Meador; A R Means; F A Quiocho
Journal:  J Mol Biol       Date:  1992-12-20       Impact factor: 5.469

6.  The crystal structure of staphylococcal nuclease refined at 1.7 A resolution.

Authors:  T R Hynes; R O Fox
Journal:  Proteins       Date:  1991

7.  Solution studies of staphylococcal nuclease H124L. 2. 1H, 13C, and 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphate-calcium ternary complex.

Authors:  J F Wang; A P Hinck; S N Loh; D M LeMaster; J L Markley
Journal:  Biochemistry       Date:  1992-01-28       Impact factor: 3.162

8.  A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

Authors:  M Ikura; L E Kay; A Bax
Journal:  Biochemistry       Date:  1990-05-15       Impact factor: 3.162

9.  Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach.

Authors:  A C de Dios; J G Pearson; E Oldfield
Journal:  Science       Date:  1993-06-04       Impact factor: 47.728

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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  12 in total

1.  Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations.

Authors:  M A McCoy; D F Wyss
Journal:  J Biomol NMR       Date:  2000-11       Impact factor: 2.835

2.  13C(alpha) and 13C(beta) chemical shifts as a tool to delineate beta-hairpin structures in peptides.

Authors:  C M Santiveri; M Rico; M A Jiménez
Journal:  J Biomol NMR       Date:  2001-04       Impact factor: 2.835

3.  An empirical correlation between secondary structure content and averaged chemical shifts in proteins.

Authors:  Anaika B Sibley; Monique Cosman; V V Krishnan
Journal:  Biophys J       Date:  2003-02       Impact factor: 4.033

4.  An evaluation of chemical shift index-based secondary structure determination in proteins: influence of random coil chemical shifts.

Authors:  S P Mielke; V V Krishnan
Journal:  J Biomol NMR       Date:  2004-10       Impact factor: 2.835

5.  C alpha and C beta carbon-13 chemical shifts in proteins from an empirical database.

Authors:  M Iwadate; T Asakura; M P Williamson
Journal:  J Biomol NMR       Date:  1999-03       Impact factor: 2.835

6.  Assignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronuclear NMR spectroscopy at natural abundance.

Authors:  C Lefevre; E Adjadj; E Quiniou; J Mispelter
Journal:  J Biomol NMR       Date:  1994-09       Impact factor: 2.835

7.  Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in monitoring a protein NMR structure refinement.

Authors:  B Celda; C Biamonti; M J Arnau; R Tejero; G T Montelione
Journal:  J Biomol NMR       Date:  1995-02       Impact factor: 2.835

8.  Predicting the redox state and secondary structure of cysteine residues using multi-dimensional classification analysis of NMR chemical shifts.

Authors:  Ching-Cheng Wang; Wen-Chung Lai; Woei-Jer Chuang
Journal:  J Biomol NMR       Date:  2016-09-09       Impact factor: 2.835

Review 9.  Chemical shifts and three-dimensional protein structures.

Authors:  E Oldfield
Journal:  J Biomol NMR       Date:  1995-04       Impact factor: 2.835

10.  High-level production of uniformly ¹⁵N- and ¹³C-enriched fusion proteins in Escherichia coli.

Authors:  M Jansson; Y C Li; L Jendeberg; S Anderson; G T Montelione; B Nilsson
Journal:  J Biomol NMR       Date:  1996-03       Impact factor: 2.835
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