NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin

Protein Science

Volumn 5, Issue 12, 1996, Pages 2552-2565

  De Lorimier, Robert ^a   Hellinga, Homme W ^a   Spicer, Leonard D ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

dynamics; hydrogen exchange; hydrophobic core; NMR; spin relaxation; structure; thioredoxin

Indexed keywords

THIOREDOXIN;

AMINO ACID SUBSTITUTION; ANION EXCHANGE; ARTICLE; CONFORMATIONAL TRANSITION; GENE DISRUPTION; GENE MUTATION; HYDROGEN BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SOLVATION;

EID: 0030475876     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051218     Document Type: Article

References (34)

1. Bai Y, Milne JS, Mayne L, Englander SW. 1993. Primary structure effects on peptide group hydrogen exchange Proteins Struct Funct Genet 17:75-86.
2. Bax A, Davis DG. 1985 MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 65.355-360.
3. 15N NMR spectra of reduced and oxidized Escherichia colt thioredoxin. FEBS Lett 284:178-183
4. 1H NMR spectroscopy. Biochemistry 29:7387-7401.
5. Connolly ML. 1983. Solvent-accessible surfaces of proteins and nucleic acids. Science 221:709-713.
6. Dao-pin S, Anderson DE, Baase WA, Dahlquist FW, Matthews BW. 1991. Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry 30:11521-11529.
7. Dyson HJ, Hoimgren A, Wright PE. 1989. Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: Sequence-specific assignments, secondary structure, and global fold. Biochemistry 28:7074-7087.
8. Englander SW, Mayne L. 1992. Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct 21:243-265.
9. 15N NMR relaxation. Biochemistry 33:5984-6003.
10. 15N relaxation data exclusively. J Biomol NMR 6:153-162.
11. Hellinga HW, Wynn R, Richards FM. 1992. The hydrophobic core of Escherichia coli thioredoxin shows a high tolerance to nonconservative single amino acid substitutions. Biochemistry 31:11203-11209.
12. Ishima R, Nagayama K. 1995. Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei. Biochemistry 34: 3162-3171.
13. Jeener J, Meier BH, Bachmann P, Ernst RR. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy J Chem Phys 71:4546-4553.
14. Jeng MF, Dyson HJ. 1995. Comparison of the hydrogen-exchange behavior of reduced and oxidized Escherichia colt thioredoxin. Biochemistry 34:611-619.
15. Katti SK, LeMaster DM, Eklund H. 1990. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J Mol Biol 212:167-184.
16. Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665.
17. 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease. Biochemistry 28:8972-8979.
18. Ladbury JE, Wynn R, Hellinga HW, Sturtevant JM. 1993. Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. Biochemistry 32:7526-7530.
19. Ladbury JE, Wynn R, Thomson JA, Sturtevant JM. 1995. Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. Biochemistry 34:2148-2152.
20. Levin MH, Freeman R, Frenkiel T. 1982. Broadband heteronuclear decoupling. J Magn Reson 47:328-330.
21. Lim WA, Farruggio DC. Sauer RT. 1992. Structural and energetic consequences of disruptive mutations in a protein core. Biochemistry 31:4324-4333.
22. Lipari G, Szabo A. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J Am Chem Soc 104:4546-4559.
23. 13C heteronuclear NMR spectroscopy. J Am Chem Soc 113:4371-4380.
24. Peng JW, Wagner G. 1992a. Mapping spectral density functions using heteronuclear NMR relaxation measurements. J Magn Reson 98:308-332.
25. Peng JW, Wagner G. 1992b. Mapping of the spectral densities of N-H bond motions m eglin c using heteronuclear relaxation experiments. Biochemistry 31.8571-8586.
26. Piantini U, Sorenson OW, Ernst RR. 1982. Multiple quantum filters for elucidating NMR coupling networks. J Am Chem Soc 104:6800-6801.
27. Ptitsyn OB. 1992. The molten globule state. In: Creighton TE, ed, Protein folding. New York: WH Freeman. pp 243-300.
28. 1H NMR spectra of proteins via double quantum filtering. Biochem Biophys Res Comm 117:479-485.
29. Richards FM. 1977. Areas, volumes, packing and protein structure. Annu Rev Biophys Bioeng 6:151-176.
30. Richards FM, Lim WA. 1994. An analysis of packing in the protein folding problem. Q Rev Biophys 26:423-498.
31. Schneider DM, Dellwo MJ, Wand AJ. 1992. Fast internal main-chain dynamics of human ubiquitin. Biochemistry 31:3645-3652.
32. Stites WE, Gittis AG, Lattman EE, Shortle D. 1991. In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core. J Mol Biol 221:7-14.
33. 15N NMR relaxation measurements. Biochemistry 32 426-435.
34. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensinvity pulsed field gradient NMR techniques. J Biomol NMR 4:845-858.