Experiments and Strategies for the Assignment of Fully 13C/15N-labelled Polypeptides by Solid State NMR

Overview

Journal J Biomol NMR

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 1998 Sep 8

PMID 9729787

Citations 24

Authors

S K Straus

T Bremi

R R Ernst

Affiliations

Soon will be listed here.

Abstract

High-resolution heteronuclear NMR correlation experiments and strategies are proposed for the assignment of fully 13C/15N-labelled polypeptides in the solid state. By the combination of intra-residue and inter-residue 13C-15N correlation experiments with 13C-13C spin-diffusion studies, it becomes feasible to partially assign backbone and side-chain resonance in solid proteins. The performance of sequences using 15N instead of 13C detection is evaluated regarding sensitivity and resolution for a labelled dipeptide (L-Val-L-Phe). The techniques are used for a partial assignment of the 15N and 13C resonances in human ubiquitin.

Citing Articles

Beyond Structural Biology to Functional Biology: Solid-State NMR Experiments and Strategies for Understanding the M2 Proton Channel Conductance.

Qin H, Miao Y, Cross T, Fu R J Phys Chem B. 2017; 121(18):4799-4809.

PMID: 28425709 PMC: 5842430. DOI: 10.1021/acs.jpcb.7b02468.

The NMR-Rosetta capsid model of M13 bacteriophage reveals a quadrupled hydrophobic packing epitope.

Morag O, Sgourakis N, Baker D, Goldbourt A Proc Natl Acad Sci U S A. 2015; 112(4):971-6.

PMID: 25587134 PMC: 4313819. DOI: 10.1073/pnas.1415393112.

Improving the quality of 2D solid-state NMR spectra of microcrystalline proteins by covariance analysis.

Weingarth M, Tekely P, Bruschweiler R, Bodenhausen G Chem Commun (Camb). 2010; 46(6):952-4.

PMID: 20107661 PMC: 2865830. DOI: 10.1039/b920844e.

Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR.

Zhang Y, Doherty T, Li J, Lu W, Barinka C, Lubkowski J J Mol Biol. 2010; 397(2):408-22.

PMID: 20097206 PMC: 2873975. DOI: 10.1016/j.jmb.2010.01.030.

Dependence of amino acid side chain 13C shifts on dihedral angle: application to conformational analysis.

London R, Wingad B, Mueller G J Am Chem Soc. 2008; 130(33):11097-105.

PMID: 18652454 PMC: 2712834. DOI: 10.1021/ja802729t.

References

Clore G, Bax A, Driscoll P, Wingfield P, Gronenborn A . Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy. Biochemistry. 1990; 29(35):8172-84. DOI: 10.1021/bi00487a027. View

Dotsch V, Matsuo H, Wagner G . Amino-acid-type identification for deuterated proteins with a beta-carbon-edited HNCOCACB experiment. J Magn Reson B. 1996; 112(1):95-100. DOI: 10.1006/jmrb.1996.0117. View

Ecker D, Khan M, Marsh J, Butt T, Crooke S . Chemical synthesis and expression of a cassette adapted ubiquitin gene. J Biol Chem. 1987; 262(8):3524-7. View

Ikura M, Kay L, Bax A . A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry. 1990; 29(19):4659-67. DOI: 10.1021/bi00471a022. View

Wand A, Urbauer J, McEvoy R, Bieber R . Internal dynamics of human ubiquitin revealed by 13C-relaxation studies of randomly fractionally labeled protein. Biochemistry. 1996; 35(19):6116-25. DOI: 10.1021/bi9530144. View

Hirsh D, Hammer J, Maloy W, Blazyk J, Schaefer J . Secondary structure and location of a magainin analogue in synthetic phospholipid bilayers. Biochemistry. 1996; 35(39):12733-41. DOI: 10.1021/bi961468a. View

Wishart D, Sykes B, Richards F . Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol. 1991; 222(2):311-33. DOI: 10.1016/0022-2836(91)90214-q. View

Pervushin K, Riek R, Wider G, Wuthrich K . Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci U S A. 1997; 94(23):12366-71. PMC: 24947. DOI: 10.1073/pnas.94.23.12366. View

Bugg C, Cook W . Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol. 1987; 194(3):531-44. DOI: 10.1016/0022-2836(87)90679-6. View

10.

Heller J, Kolbert A, Larsen R, Ernst M, Bekker T, Baldwin M . Solid-state NMR studies of the prion protein H1 fragment. Protein Sci. 1996; 5(8):1655-61. PMC: 2143492. DOI: 10.1002/pro.5560050819. View

11.

Tycko R . Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins. J Biomol NMR. 1996; 8(3):239-51. DOI: 10.1007/BF00410323. View

12.

Kay L . Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution. Prog Biophys Mol Biol. 1995; 63(3):277-99. DOI: 10.1016/0079-6107(95)00007-0. View

13.

Tjandra N, Bax A . Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science. 1997; 278(5340):1111-4. DOI: 10.1126/science.278.5340.1111. View

14.

Lansbury Jr P, Costa P, Griffiths J, Simon E, Auger M, Halverson K . Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat Struct Biol. 1995; 2(11):990-8. DOI: 10.1038/nsb1195-990. View