Rapid and accurate processing method for amide proton exchange rate measurement in proteins

Journal of Biomolecular NMR

Volumn 37, Issue 4, 2007, Pages 313-320

  Koskela, Harri ^a   Heikkinen, Outi ^a   Kilpeläinen, Ilkka ^a   Heikkinen, Sami ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Exchange resolved 15N HSQC; Gifa; Inverse Laplace transform; Protein backbone amide hydrogen exchange; Saturation transfer; Ubiquitin

Indexed keywords

UBIQUITIN;

ARTICLE; COMPUTER ANALYSIS; DIAGNOSTIC ACCURACY; HUMAN; MATHEMATICAL ANALYSIS; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON TRANSPORT;

AMIDES; MODELS, CHEMICAL; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEINS; PROTONS;

EID: 33847787871     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-007-9145-y     Document Type: Article

References (20)

1. Delsuc MA, Malliavin TE (1998) Maximum entropy processing of DOSY NMR spectra. Anal Chem 70:2146-2148
2. Dempsey CE (2001) Hydrogen exchange in peptides and proteins using NMR spectroscopy. Prog NMR Spectrosc 39:135-170
3. Fylstra D, Lasdon L, Warren A, Watson J (1998) Design and use of the Microsoft Excel Solver. Interfaces 28:29-55
4. Garcia LIR, Volpi L (2006) Levenberg-Marquardt algorithm v14.04.2006, http://digilander.libero.it/foxes
5. Goddard TD, Kneller DG (2004) SPARKY 3. San Francisco, University of California,
6. Hwang T-L, Mori S, Shaka AJ, van Zijl PCM (1997) Application of Phase-Modulated CLEAN chemical EXchange spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs. J Am Chem Soc 119:6203-6204
7. Jerschow A, Müller N (1998) Diffusion-separated nuclear magnetic resonance spectroscopy of polymer mixtures. Macromolecules 31:6573-6578
8. Johnson CS Jr, (1999) Diffusion ordered nuclear magnetic resonance spectroscopy: Principles and applications. Prog NMR Spectrosc 34:203-256
9. Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637
10. Kay LE, Ikura M, Tschudin R, Bax A (1990) Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J Magn Reson 89:496-514
11. 15N relaxation times by inverse Laplace transformation. Magn Reson Chem 42:61-65
12. Lasdon LS, Waren AD, Jain A, Ratner M (1978) Design and testing of a generalized reduced gradient code for nonlinear programming. ACM Trans Math Softw 4:34-50
13. Leijon M (1996) Proton exchange rates measured by saturation transfer using delayed randomization of the solvent magnetization. J Magn Reson B112:181-185
14. Marion D, Ikura M, Tschudin R, Bax A (1989) Rapid recording of 2D NMR spectra without phase cycling: Application to the study of hydrogen exchange in proteins. J Magn Reson 85:393-399
15. Nakamura F, Pudas R, Heikkinen O, Permi P, Kilpeläinen I, Munday AD, Hartwig JH, Stossel TP, Ylänne J (2006) The structure of the GPIb-filamin A complex. Blood 107:1925-1932
16. Palmer III AG, Cavanagh J, Wright PE, Rance M (1991) Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J Magn Reson 93:151-170
17. Pons LJ, Malliavin TE, Delsuc MA (1996) Gifa V. 4: A complete package for NMR data set processing. J Biomol NMR 8:445-452
18. Shaka AJ, Barker PB, Freeman R (1985) Experimental demonstration of wideband spin inversion. J Magn Reson 64:547-552
19. Volpi L (2006) Optimiz.xla v.2.0, http://digilander.libero.it/foxes
20. Wójcik J, Ruszczynska K, Zhukov I, Ejchart A (1999) NMR measurements of proton exchange between solvent and peptides and proteins. A Biochim Pol 46:651-663