Role of a salt bridge in the model protein crambin explored by chemical protein synthesis: X-ray structure of a unique protein analogue, [V15A]crambin-α-carboxamide

Molecular BioSystems

Volumn 5, Issue 7, 2009, Pages 750-756

  Bang, Duhee ^a,b   Tereshko, Valentina ^a,b   Kossiakoff, Anthony A ^a,b   Kent, Stephen B H ^a,b  

^a UNIVERSITY OF CHICAGO   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARAGINE; CRAMBIN PROTEIN, CRAMBE ABYSSINICA; VEGETABLE PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; MASS SPECTROMETRY; METABOLISM; METHODOLOGY; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SYNTHESIS; X RAY CRYSTALLOGRAPHY;

ARGININE; ASPARAGINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CRYSTALLOGRAPHY, X-RAY; KINETICS; MASS SPECTROMETRY; MODELS, MOLECULAR; PLANT PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 67650367214     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/b903610e     Document Type: Article

References (27)

1. M. F. Perutz Electrostatic effects in proteins Science 1978 201 1187 1191
2. A. Bierzynski P. S. Kim R. L. Baldwin A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A Proc. Natl. Acad. Sci. U. S. A. 1982 79 2470 2474
3. B. W. Matthews Structural and genetic analysis of protein stability Annu. Rev. Biochem. 1993 62 139 160
4. C. A. Blasie J. M. Berg Electrostatic interactions across a beta-sheet Biochemistry 1997 36 6218 6222
5. P. Strop S. L. Mayo Contribution of surface salt bridges to protein stability Biochemistry 2000 39 1251 1255
6. G. I. Makhatadze V. V. Loladze D. N. Ermolenko X. Chen S. T. Thomas Contribution of surface salt bridges to protein stability: guidelines for protein engineering J. Mol. Biol. 2003 327 1135 1148
7. S. S. Strickler A. V. Gribenko A. V. Gribenko T. R. Keiffer J. Tomlinson T. Reihle V. V. Loladze G. I. Makhatadze Protein stability and surface electrostatics: a charged relationship Biochemistry 2006 45 2761 2766
8. A. V. Gribenko M. M. Patel J. Liu S. A. McCallum C. Wang G. I. Makhatadze Rational stabilization of enzymes by computational redesign of surface charge-charge interactions Proc. Natl. Acad. Sci. U. S. A. 2009 106 2601 2606
9. C. H. VanEtten H. C. Nielsen J. E. Peters A crystalline polypeptide from the seed of Crambe abyssinica Phytochemistry 1965 4 467 473
10. M. M. Teeter J. A. Mazer J. J. L'Italien Primary structure of the hydrophobic plant protein crambin Biochemistry 1981 20 5437 5443
11. C. Jelsch M. M. Teeter V. Lamzin V. Pichon-Pesme R. H. Blessing C. Lecomte Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin Proc. Natl. Acad. Sci. U. S. A. 2000 97 3171 3176
12. F. H. Arnold Protein design for non-aqueous solvent Protein Eng. 1988 2 21 25
13. L. Lobb B. Stec E. K. Kantrowitz A. Yamano V. Stojanoff O. Markman M. M. Teeter Expression, purification and characterization of recombinant crambin Protein Eng. 1996 9 1233 1239
14. H. C. Ahn N. Juranić S. Macura J. L. Markley Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface J. Am. Chem. Soc. 2006 128 4398 4404
15. P. E. Dawson S. B. Kent Synthesis of native proteins by chemical ligation Annu. Rev. Biochem. 2000 69 923 960
16. S. B. Kent Total chemical synthesis of proteins Chem. Soc. Rev. 2009 38 338 351
17. D. Bang C. Neeraj S. B. Kent J. Am. Chem. Soc. 2004 126 1377 1383
18. M. Schnölzer P. Alewood A. Jones D. Alewood S. B. Kent In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences Int. J. Pept. Res. Ther. 2007 13 31 44
19. D. Bang S. B. Kent A one-pot synthesis of crambin Angew. Chem., Int. Ed. 2004 43 2534 2538
20. A. T. Brunger P. D. Adams G. M. Clore W. L. Delano P. Gros R. W. Grosse-Kunstleve J.-S. Jinang J. Kuszewski N. Nilges N. S. Pannu R. J. Read L. M. Rice T. Simonson G. L. Warren Crystallography and NMR system (CNS): a new software system for macromolecular structure determination Acta Crystallogr., Sect. D: Biol. Crystallogr. 1998 54 905 921
21. G. N. Murshudov A. A. Vagin E. J. Dodson Refinement of macromolecular structures by maximum-likelihood method Acta Crystallogr., Sect. D: Biol. Crystallogr. 1997 53 240 255
22. P. E. Dawson T. W. Muir I. Clark-Lewis S. B. Kent Synthesis of proteins by native chemical ligation Science 1994 266 776 779
23. Z. Otwinowski W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 1997 276 307 326
24. A. A. Vagin A. Teplyakov MOLREP: An Automated Program for Molecular Replacement J. Appl. Crystallogr. 1997 30 1022 1025
25. Collaborative Computational Project The CCP4 Suite: Programs for Protein Crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994 50 760 763
26. M. Carson Ribbons Methods Enzymol. 1997 277 493 505
27. C. Cambillau and A. Roussel, Turbo Frodo, version OpenGL.1., University Aix-Marseille II, Marseille, 1997