Ionization behavior of acidic residues in calbindin D(9k)

Proteins: Structure, Function and Genetics

Volumn 37, Issue 1, 1999, Pages 106-115

  Kesvatera, Tõnu ^a,b   Jönsson, Bo ^a   Thulin, Eva ^a   Linse, Sara ^a  

^a LUND UNIVERSITY   (Sweden)

^b NATIONAL INSTITUTE OF CHEMICAL PHYSICS AND BIOPHYSICS   (Estonia)

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; ASPARTIC ACID; CALBINDIN; CALCIUM ION; CARBOXYL GROUP; GLUTAMIC ACID; LIGAND;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATTLE; CONTROLLED STUDY; IONIZATION; ISOELECTRIC POINT; NONHUMAN; PH; PKA; PRIORITY JOURNAL; SYSTEM ANALYSIS;

ANIMALS; CALCIUM-BINDING PROTEIN, VITAMIN D-DEPENDENT; CATTLE; ELECTROSTATICS; HYDROGEN-ION CONCENTRATION; MONTE CARLO METHOD; PROTEIN CONFORMATION;

BOS TAURUS; BOVINAE;

EID: 0344500828     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991001)37:1<106::AID-PROT10>3.0.CO;2-M     Document Type: Article

References (46)

1. Antosiewicz J, McCammon JA, Gilson MK. Prediction of pH-dependent properties of proteins. J Mol Biol 1994;238:415-436.
2. 9k. J Mol Biol 1996;259:828-839.
3. Dimitrov RA, Crichton RR. Self-consistent field approach to protein structure and stability. I. pH dependence of electrostatic contribution. Proteins Struct Funct Genet 1997;27:576-596.
4. Juffer AH, Argos P, Vogel HJ. Calculating acid-dissociation constants of proteins using the boundary element method. J Phys Chem B 1997;101:7664-7673.
5. a measurements from nuclear magnetic resonance for the B1 and B2 immunoglobulin G-binding domains of protein G: comparison with calculated values for nuclear magnetic resonance and x-ray structures. Biochemistry 1997;36:3580-3589.
6. Forsén S, Kördel J, Grundström T, Chazin WJ. The molecular anatomy of a calcium-binding protein. Acc Chem Res 1997; 26:7-14.
7. 1H-NMR spectroscopy. Proc Natl Acad Sci USA 1989;86:2195-2198.
8. 9k modified in the pseudo EF-hand. Eur J Biochem 1990;187:455-460.
9. Bax A, Ikura M, Kay LE, Torchia DA, Tscudin R. Comparison of different models of two-dimensional reverse-correlation NMR for the study of proteins. J Magn Reson 1990;86:304-318.
10. 15N spectroscopy. J Magn Reson 1990;87:488-501.
11. Braunschweiler L, Ernst RR. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J.Magn Reson 1983;53:521-528.
12. Rance M. Improved techniques for homonuclear rotating-frame and isotropic mixing experiments. J Magn Reson 1987;74:557-564.
13. Shaka AJ, Barker PB, Freeman R. Computer-optimized decoupling scheme for wideband applications and low-level operation. J Magn Reson 1985;64:547-552.
14. Shaka AJ, Lee CJ, Pines A. Iterative schemes for bilinear operators; application to spin decoupling. J Magn Reson 1988;77:274-293.
15. Schleucher J, Schwendinger M, Sattler M, et al. A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients. J Biomol NMR 1994;4:301-306.
16. 3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 1994;4:845-858.
17. 9k. Biochemistry 1990;29:5752-5761.
18. Szebenyi DME, Moffat K. The refined structure of vitamin D dependent calcium-binding protein from bovine intestine: molecular details, ion binding, and implications for the structure of other calcium-binding proteins. J Biol Chem 1986;261:8671-8777.
19. Metropolis N, Rosenbluth AW, Rosenbluth MN, Teller AH, Teller E. Equation of state calculations by fast computing machines. J Chem Phys 1953;21:1087-1092.
20. Nozaki Y, Tanford C. Examination of titration behavior. Methods Enzymol 1967;11:715-734.
21. Widom B. Some topics in the theory of fluids. J Chem Phys 1963;39:2808-2812.
22. 9k: a Monte Carlo simulation study. Biochemistry 1991;30:5209-5217.
23. 9k: structural stability and function at high salt concentration. Biochemistry 1994;33:14170-14176.
24. a values of the lysine residues in calmodulin. J Biol Chem 1993;268:22420-22428.
25. 9k. J Protein Chem 1994;13:527-535.
26. Linse S, Jönsson BO, Chazin WJ. The effect of protein concentration on ion binding. Proc Natl Acad Sci USA 1995;92:4748-4752.
27. Anderson DE, Lu J, McIntosh LP, Dahlquist FW. The folding, stability and dynamics of T4 lysozyme: a perspective using nuclear magnetic resonance. In: Clore GM, Gronenborn AM, editors. NMR of Proteins. London: MacMillan Press; 1993. p. 258-304.
28. 13C-NMR study of Bacillus circulans xylanase. Biochemistry 1996;35:9958-9966.
29. a values of the carboxyl and imidazole groups in Bacillus circulans xylanase. Protein Sci 1997;6:2667-2670.
30. Yamazaki T, Nicholson LK, Torchia DA, et al. NMR and X-ray evidence that the HIV protease catalytic aspartyl groups are protonated in the complex formed by the protease and a non-peptide cyclic urea-based inhibitor. J Am Chem Soc 1994;116: 10791-10792.
31. 13C nuclear magnetic resonance studies at 90.5 Mhz of the basic pancreatic trypsin inhibitor. Biochemistry 1978;17:2263-2269.
32. Markley JL. Observation of histidine residues in proteins by means of nuclear magnetic resonance spectroscopy. Acc Chem Res 1975;8:70-80.
33. Shrager RI, Cohen JS, Heller SR, Sachs DH, Schecher AN. Mathematical models for interacting groups in nuclear magnetic resonance titration curves. Biochemistry 1972;11:541-547.
34. 9k by NMR spectroscopy. J Mol Biol 1995;249:441-462.
35. 9k. Eu. J Biochem 1988;175:435-445.
36. 2+-binding proteins. Nat Struct Biol 1994;1:239-245.
37. Antosiewicz J, Gilson MK, McCammon JA. Acetylcholinesterase: effects of ionic strength and dimerization on the rate constants. Isr J Chem 1994;34:151-158.
38. 2- to calmodulin and its tryptic fragments: theory and experiment. Biochemistry 1993;32:2828-2834.
39. Smith PE, Brunne RM, Mark AE, van Gunsteren WF. Dielectric properties of trypsin inhibitor and lysozyme calculated from molecular dynamics. J Phys Chem 1993;97:2009-2014.
40. a's of ionizable residues in proteins: semi-microscopic and macroscopic approaches. J Phys Chem B 1997;101:4458-4472.
41. Warshel A, Åquist J. Electrostatic energy and macromolecular function. Annu Rev Biophys Chem 1991;20:267-298.
42. Warshel A, Russell ST, Churg AK. Macroscopic models for studies of electrostatic interactions in proteins: limitations and applicability. Proc Natl Acad Sci USA 1984;81:4785-4789.
43. Tanford C. The location of electrostatic charges in Kirkwood's model of organic ons, J Am Chem Soc 1957;79: 5348-5352.
44. Ullner, M., Jönsson B. A Monte Carlo study of titrating polyelectrolytes in the presence of salt. Macromolecules 1996;29:6645-6655.
45. Spassov V, Bashford D. Electrostatic coupling to pH-titrating sites as a source of cooperativity in protein-ligand binding. Protein Sci 1998;7:2012-2025.
46. de Groot J, Koper GJM, Borhovec M, de Bleijser J. Dissociation behavior of poly(maleic acid): potentiometric titrations, viscometry, pulsed field gradient NMR, and model calculations. Macromolecules 1998;31:4182-4188.