Literature DB >> 8400833

A simple and sensitive experiment for measurement of JCC couplings between backbone carbonyl and methyl carbons in isotopically enriched proteins.

S Grzesiek1, G W Vuister, A Bax.   

Abstract

A simple 2D difference experiment is described that allows quantitative measurement of 13C-13C J couplings between backbone carbonyl and side-chain carbons. Precise 3JCC values were measured from data recorded in just 2 h for a 1-mM solution of the 20-kD complex between the protein calmodulin and a 26-residue synthetic peptide. The J couplings aid in determining the chi 1 angles of valine, isoleucine and threonine residues, and in making stereospecific assignments of the Val C gamma methyl groups. Error analysis indicates that the uncertainty in the derived J couplings is generally less than ca. 0.3 Hz.

Entities:  

Mesh:

Substances:

Year:  1993        PMID: 8400833     DOI: 10.1007/bf00176014

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


  4 in total

1.  Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.

Authors:  W E Meador; A R Means; F A Quiocho
Journal:  Science       Date:  1992-08-28       Impact factor: 47.728

2.  Solution structure of a calmodulin-target peptide complex by multidimensional NMR.

Authors:  M Ikura; G M Clore; A M Gronenborn; G Zhu; C B Klee; A Bax
Journal:  Science       Date:  1992-05-01       Impact factor: 47.728

3.  Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formation.

Authors:  R E Klevit; D K Blumenthal; D E Wemmer; E G Krebs
Journal:  Biochemistry       Date:  1985-12-31       Impact factor: 3.162

4.  Quantitative measurement of small through-hydrogen-bond and 'through-space' 1H-113Cd and 1H-199Hg J couplings in metal-substituted rubredoxin from Pyrococcus furiosus.

Authors:  P R Blake; B Lee; M F Summers; M W Adams; J B Park; Z H Zhou; A Bax
Journal:  J Biomol NMR       Date:  1992-09       Impact factor: 2.835

  4 in total
  43 in total

1.  Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain.

Authors:  G Barbato; D O Cicero; F Cordier; F Narjes; B Gerlach; S Sambucini; S Grzesiek; V G Matassa; R De Francesco; R Bazzo
Journal:  EMBO J       Date:  2000-03-15       Impact factor: 11.598

2.  Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.

Authors:  Vadim Gaponenko; Siddhartha P Sarma; Amanda S Altieri; David A Horita; Jess Li; R Andrew Byrd
Journal:  J Biomol NMR       Date:  2004-03       Impact factor: 2.835

3.  The solution structure of the anti-HIV chemokine vMIP-II.

Authors:  A C Liwang; Z X Wang; Y Sun; S C Peiper; P J Liwang
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

4.  Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR.

Authors:  Zhengrong Wu; Frank Delaglio; Keith Wyatt; Graeme Wistow; Ad Bax
Journal:  Protein Sci       Date:  2005-10-31       Impact factor: 6.725

5.  The structure of phospholamban pentamer reveals a channel-like architecture in membranes.

Authors:  Kirill Oxenoid; James J Chou
Journal:  Proc Natl Acad Sci U S A       Date:  2005-07-25       Impact factor: 11.205

6.  Dynamic coupling and allosteric behavior in a nonallosteric protein.

Authors:  Michael W Clarkson; Steven A Gilmore; Marshall H Edgell; Andrew L Lee
Journal:  Biochemistry       Date:  2006-06-27       Impact factor: 3.162

7.  Factors affecting the use of 13C(alpha) chemical shifts to determine, refine, and validate protein structures.

Authors:  Jorge A Vila; Harold A Scheraga
Journal:  Proteins       Date:  2008-05-01

8.  Monomeric solution structure of the prototypical 'C' chemokine lymphotactin.

Authors:  E S Kuloglu; D R McCaslin; M Kitabwalla; C D Pauza; J L Markley; B F Volkman
Journal:  Biochemistry       Date:  2001-10-23       Impact factor: 3.162

9.  Accurate measurement of methyl 13C chemical shifts by solid-state NMR for the determination of protein side chain conformation: the influenza a M2 transmembrane peptide as an example.

Authors:  Mei Hong; Tatiana V Mishanina; Sarah D Cady
Journal:  J Am Chem Soc       Date:  2009-06-10       Impact factor: 15.419

10.  Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle.

Authors:  Lisa M Tuttle; H Jane Dyson; Peter E Wright
Journal:  Biochemistry       Date:  2013-05-07       Impact factor: 3.162

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.