Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation

Proteins: Structure, Function and Genetics

Volumn 40, Issue 1, 2000, Pages 29-38

  Muzammil, Salman ^a,b   Kumar, Yogesh ^a   Tayyab, Saad ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

^b MEDICAL COLLEGE OF GEORGIA   (United States)

Author keywords

Anion induced stabilization; ANS fluorescence; Circular dichroism; Human serum albumin; Intermediate state; Protein folding

Indexed keywords

ACRYLAMIDE; ANION; ANION EXCHANGE RESIN; HUMAN SERUM ALBUMIN; POTASSIUM CHLORIDE; POTASSIUM DERIVATIVE; SODIUM DERIVATIVE; TRYPTOPHAN; UREA;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; FLUORESCENCE; HYDRATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY;

ANION EXCHANGE RESINS; ANIONS; CIRCULAR DICHROISM; HUMANS; INDICATORS AND REAGENTS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SERUM ALBUMIN; UREA;

EID: 0034237709     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000701)40:1<29::AID-PROT50>3.0.CO;2-P     Document Type: Article

References (62)

1. Nolting B, Golbik R, Fersht AR. Submillisecond events in protein folding. Proc Natl Acad Sci USA 1995;92:10668-10672.
2. Plaxco KW, Dobson CM. Time-resolved biophysical methods in the study of protein folding. Curr Opin Struct Biol 1996;6:630-636.
3. Ptitsyn OB. Kinetic and equilibrium intermediates in protein folding. Protein Eng 1994;7:593-596.
4. Radford SE, Dobson CM. Insights into protein folding using physical techniques: Studies of lysozyme and α-lactalbumin. Phil Trans R Soc Lond B 1995;348:17-25.
5. Privalov PL. Intermediate states in protein folding. J Mol Biol 1996;258:707-725.
6. Jaenicke R. Oligomeric proteins. In: Fink AL, Goto Y, editors. Molecular chaperones in the life cycle of proteins. Structure, function and mode of action. New York: Marcel Dekker Inc;1998. p 35-70.
7. Wetlaufer DB. Folding of protein fragments. Adv Protein Chem 1981;34:61-92.
8. Privalov PL. Stability of proteins which do not present a single cooperative unit. Adv Protein Chem 1982;35:1-104.
9. Jaenicke R, Seckler R. Protein misassembly in vitro. Adv Protein Chem 1997;50:1-59.
10. von Hippel PH, Schleich T. The effects of neutral salts on the structure and conformational stability of macromolecules in solution. In: Timasheff SN, Fasman GD, editors. Structure and stability of biological macromolecules. New York: Marcel Dekker Inc; 1969. p 417-574.
11. Arakawa T, Bhat R, Timasheff SN. Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry 1990;29:1924-1931.
12. Schellman JA. Selective binding and solvent denaturation. Biopolymers 1987;26:549-559.
13. Schellman JA. A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures. Biophys Chem 1990;37:121-140.
14. Timasheff SN. Water as ligand: Preferential binding and exclusion of denaturants in protein unfolding. Biochemistry 1992;31: 9857-9864.
15. Timasheff SN. Solvent stabilization of protein structure. Methods Mol Biol 1995;40:253-269.
16. Yang AS, Honig B. Electrostatic effects on protein stability. Curr Opin Struct Biol 1992;2:40-45.
17. Gilson MK. Theory of electrostatic interactions in macromolecules. Curr Opin Struct Biol 1995;5:216-223.
18. Pace CN, Grimsley GR. Ribonuclease T1 is stabilized by cation and anion binding. Biochemistry 1988;27:3242-3246.
19. Makhatadze GI, Lopez MM, Richardson JM III, Thomas ST. Anion binding to the ubiquitin molecule. Protein Sci 1998;7:689-697.
20. Carter DC, Ho JX. Structure of serum albumin. Adv Protein Chem 1994;45:153-203.
21. He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature 1992;358:209-215.
22. King TP, Spencer M. Structural studies and organic ligand-binding properties of bovine plasma albumin. J Biol Chem 1970; 245:6134-6148.
23. Reed RG, Feldhoff RC, Clute OL, Peters T Jr. Fragments of bovine serum albumin produced by limited proteolysis. Conformation and ligand binding. Biochemistry 1975;14:4578-4583.
24. Kjeldsen T, Pettersson AF, Drube L, Kurtzhals P, Jonassen I, Havelund S, Hansen PH, Markussen J. Secretory expression of human albumin domains in Saccharomyces cerevisiae and their binding of myristic acid and an acylated insulin analogue. Prot Express Purif 1998;13:163-169.
25. Khan MY, Agarwal SK, Hangloo S. Urea-induced structural transformations in bovine serum albumin. J Biochem 1987;102: 313-317.
26. Chmelik J, Anzenbacher P, Chmelikova J. Mechanism of denaturation of human serum albumin by urea. Coll Czech Chem Commun 1988;53:411-422.
27. Wallevik K. Reversible denaturation of human serum albumin by pH, temperature and guanidine hydrochloride followed by optical rotation. J Biol Chem 1973;248:2650-2655.
28. Arakawa T, Timasheff SN. Protein stabilization and destabilization by guanidinium salts. Biochemistry 1984;23:5924-5929.
29. Mayr LM, Schmid FX. Stabilization of a protein by guanidinium chloride. Biochemistry 1993;32:7994-7998.
30. Smith JS, Scholtz JM. Guanidine hydrochloride unfolding of peptide helices: Separation of denaturant and salt effects. Biochemistry 1996;35:7292-7297.
31. Mulqueen PM, Kronman MJ. Binding of naphthalene dyes to the N and A conformers of bovine α-lactalbumin. Arch Biochem Biophys 1982;215:28-39.
32. Warren JR, Gordon JA. On the refractive indices of aqueous solutions of urea. J Phys Chem 1966;70:297-300.
33. Nozaki Y. The preparation of guanidine hydrochloride. Methods Enzymol 1972;26:43-50.
34. Pace CN, Scholtz JM. Measuring the conformational stability of a protein. In: Creighton TE, editor. Protein structure: a practical approach. New York: Oxford University Press; 1997. p 299-321.
35. Bychkova VE, Berni R, Rossi GL, Kutyshenko VP, Ptitsyn OB. Retinol-binding protein is in the molten globule state at low pH. Biochemistry 1992;31:7566-7571.
36. Eftink MR, Ghiron CA. Fluorescence quenching studies with proteins. Anal Biochem 1982;114:199-227.
37. Tanford C. Protein denaturation. Adv Protein Chem 1968;23:121-282.
38. Pace CN. Measuring and increasing protein stability. Trends Biotech 1990;8:93-98.
39. Chen Y-H, Yang JT, Martinez HM. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 1972;11:4120-4131.
40. Eftink MR. Fluorescence techniques for studying protein structure. Methods Biochem Anal 1991;35:127-205.
41. Tanaka N, Nishizawa H, Kunugi S. Structure of pressure-induced denatured state of human serum albumin: A comparison with the intermediate in urea-induced denaturation. Biochim Biophys Acta 1997; 1338:13-20.
42. Smith LJ, Fiebig KM, Schwalbe H, Dobson CM. The concept of a random coil. Residual structure in peptides and denatured proteins. Folding Des 1996;1:R95-R106.
43. Bierzynski A, Baldwin RL. Local secondary structure in ribonuclease A denatured by guanidine.HCl near 1 degree C. J Mol Biol 1982;162:173-186.
44. Amir D, Haas E. Reduced bovine pancreatic trypsin inhibitor has a compact structure. Biochemistry 1988;27:8889-8893.
45. Peters T Jr. Serum albumin. Adv Protein Chem 1985;37:161-245.
46. Ahmad Z, Ahmad F. Physico-chemical characterization of products of unfolding of cytochrome c by calcium chloride. Biochim Biophys Acta 1994;1207:223-230.
47. Halle B, Lindman B. Chloride ion binding to human plasma albumin from chlorine-35 quadrupole relaxation. Biochemistry 1978;17:3774-3781.
48. Kumar TK, Jayaram G, Lin WY, Yu C. Effect of chaotropic denaturant on the binding of 1-anilino 8-naphthalene sulfonic acid to proteins. Biochim Biophys Acta 1996;1294:103-105.
49. Collins KD, Washabaugh MW. The Hofmeister effect and the behavior of water at interfaces. Q Rev Biophys 1985;18:323-422.
50. Arakawa T, Timasheff SN. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 1982;21:6545-6552.
51. Lee JC, Timasheff SN. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry 1974;13:257-265.
52. Gregor HP, Belle J, Marcus RA. Studies on ion-exchange resins. XIII. Selectivity coefficient of quaternary base anion-exchange resins towards univalent anions. J Am Chem Soc. 1955;77:2713-2719.
53. Damodaran S. Influence of protein conformation on its adaptability under chaotropic conditions. Int J Biol Macromol 1989;11:2-8.
54. Greene RF, Pace CN. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J Biol Chem 1974;249:5388-5393.
55. Robinson DR, Jencks WP. The effect of compounds of the urea-guanidinium class on the activity coefficients of acetyltetraglycine ethyl ester and related compounds J Am Chem Soc 1965;87:2462-2470
56. Roseman M, Jencks WP. Interactions of urea and other polar compounds in water. J Am Chem Soc 1975;97:631-640.
57. Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 1986;131: 266-280.
58. Mayo SL, Baldwin RL. Guanidinium chloride induction of partial unfolding in amide proton exchange in RNAse A. Science 1993;262: 873-876.
59. Monera OD, Kay CM, Hodges RS. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci 1994;3:1984-1991.
60. Jaenicke R. Protein folding and association: In vitro studies for self-organization and targeting in the cell. In: Stadtman ER, Chock PB, editors. Current topics in cellular regulation, vol 34. New York: Academic Press Inc; 1996. p 209-314.
61. Rudolph R, Siebendritt R, Nesslauer G, Sharma AK, Jaenicke R. Folding of an all-β protein: Independent domain folding in γII-crystallin from calf eye lens. Proc Natl Acad Sci USA 1990;87:4625-4629
62. Peters T Jr. All about albumin. Biochemistry, genetics and medical applications. San Diego, CA: Academic Press Inc; 1996. 133 p.