Equilibrium unfolding of A. niger RNase: PH dependence of chemical and thermal denaturation

European Biophysics Journal

Volumn 40, Issue 8, 2011, Pages 923-935

  Kumar, Gundampati Ravi ^a   Sharma, Anurag ^b   Kumari, Moni ^b   Jagannadham, Medicherla V ^b   Debnath, Mira ^a  

^a BANARAS HINDU UNIVERSITY   (India)

^b BANARAS HINDU UNIVERSITY   (India)

Author keywords

ANS binding; Circular dichroism; Molten globule state; RNase T2 family; Unfolding

Indexed keywords

GUANIDINE; RIBONUCLEASE; RIBONUCLEASE T(2); UREA;

ARTICLE; ASPERGILLUS NIGER; CHEMISTRY; CIRCULAR DICHROISM; DRUG EFFECT; GENETICS; KINETICS; PH; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN UNFOLDING; SPECTROFLUOROMETRY; TEMPERATURE; THERMODYNAMICS; ULTRAVIOLET SPECTROPHOTOMETRY;

ASPERGILLUS NIGER; CIRCULAR DICHROISM; ENDORIBONUCLEASES; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN UNFOLDING; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; TEMPERATURE; THERMODYNAMICS; UREA;

EID: 79961026029     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-011-0708-1     Document Type: Article

References (37)

1. MA Andrade P Chacon JJ Merelo F Moran 1993 Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network Protein Eng 6 383 390 8332596 10.1093/protein/6.4.383 1:CAS:528:DyaK3sXkvFSmsbg%3D (Pubitemid 23197398)
2. D Balasubramanian C Kumar 1976 Recent studies of the circular dichroism and optical rotatory dispersion of biopolymers Appl Spec Rev 11 223 286 10.1080/05704927608060379 1:CAS:528:DyaE28XhsValtLw%3D
3. RL Baldwin GD Rose 1999 Is protein folding hierarchic? II. Folding intermediates and transition states Trends Biochem Sci 24 77 83 10098403 10.1016/S0968-0004(98)01345-0 1:CAS:528:DyaK1MXltFCgsrw%3D (Pubitemid 29346578)
4. D Barrick RL Baldwin 1993 Three-state analysis of sperm whale apomyoglobin folding Biochemistry 32 3790 3796 8466917 10.1021/bi00065a035 1:CAS:528:DyaK3sXhvVKiurw%3D (Pubitemid 23126958)
5. DR Booth M Sunde V Bellotti CV Robinson ML Hutchinson PE Fraser, et al. 1997 Instability, unfolding and aggregation of human lysozyme variants underlying amyloidosis Nature 385 787 793 9039909 10.1038/385787a0 1:CAS:528:DyaK2sXhsFWqtLY%3D (Pubitemid 27106061)
6. RA Deshpande MI Khan V Shankar 2003 Equilibrium unfolding of RNase Rs from Rhizopus stolonifer: pH dependence of chemical and thermal denaturation Biochim Biophys Acta 1648 184 194 12758161 1:CAS:528:DC%2BD3sXjvFWmu7k%3D (Pubitemid 38234620)
7. KA Dill HS Chan 1997 From Levinthal to pathways to funnels Nat Struct Biol 4 10 19 8989315 10.1038/nsb0197-10 1:CAS:528:DyaK2sXis1Ontw%3D%3D (Pubitemid 27020916)
8. WA Eaton V Munõz SJ Hagen GS Jas LJ Lapidus ER Henry J Hofrichter 2000 Annu Rev Biophys Biomol Struct 29 327 359 10940252 10.1146/annurev.biophys. 29.1.327 1:CAS:528:DC%2BD3cXlsFOnuro%3D (Pubitemid 30599597)
9. Fersht AR (1999) Protein stability. In: Julet MR (ed) Structure and mechanism in protein science. Freeman WH and Company, New York, pp 508-570
10. AL Fink 1995 Compact intermediate states in protein folding Annu Rev Biomol Struct 24 495 522 10.1146/annurev.bb.24.060195.002431 1:CAS:528:DyaK2MXmt1amsb8%3D
11. Freifelder D (1982) Physical biochemistry: applications to biochemistry and molecular biology, 2nd edn. Freeman, USA
12. RK Gundampati A Sharma M Kumari M Debnath 2011 Extracellular poly (A) specific ribonuclease from Aspergillus niger ATCC 26550: purification, biochemical, and spectroscopic studies Process Biochem 46 135 141 10.1016/j.procbio.2010.07.029 1:CAS:528:DC%2BC3cXhsF2gsL%2FP
13. CJ Halfman T Nishida 1971 Nature of the alteration of the fluorescence spectrum of bovine serum albumin produced by binding of dodecyl sulphate Biochim Biophys Acta 243 294 303 5166230 1:CAS:528:DyaE38Xit1WjtA%3D%3D
14. FU Hartl R Hlodam T Langer 1991 Molecular chaperones in protein folding: the art of avoiding sticky situations Trends Biochem Sci 19 20 25 10.1016/0968-0004(94)90169-4 (Pubitemid 24028727)
15. SE Jackson 1998 How do small single domain proteins fold? Fold Des 3 R81 R91 9710577 10.1016/S1359-0278(98)00033-9 1:CAS:528:DyaK1cXlsFSqtbs%3D (Pubitemid 28366044)
16. R Khurana JB Udgaonkar 1994 Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule Biochemistry 33 106 115 8286327 10.1021/bi00167a014 1:CAS:528: DyaK2cXkvVOntw%3D%3D (Pubitemid 24046502)
17. PS Kim RL Baldwin 1990 Intermediates in folding reactions of small proteins Ann Rev Biochem 59 631 652 2197986 10.1146/annurev.bi.59.070190.003215 1:CAS:528:DyaK3cXls1Ontro%3D
18. K Kuwajima 1992 Protein folding in vitro Curr Opin Biotechnol 3 462 467 1368930 10.1016/0958-1669(92)90072-Q 1:CAS:528:DyaK38XmsVOhs7g%3D
19. Kuwajima K, Arai M (1999) Old and new views of protein folding. Elsevier, The Netherlands
20. P Manavalan WC Johnson 1983 Sensitivity of circular dichroism to protein tertiary structure class Nature 305 831 832 10.1038/305831a0 1:CAS:528:DyaL3sXmtVygsbk%3D
21. CR Matthews 1995 Pathways of protein folding Annu Rev Biochem 62 653 683 10.1146/annurev.bi.62.070193.003253
22. JM Matthews RS Norton A Hammacher RJ Simpson 2000 The single mutation Phe173 → Ala induces a molten globule-like state in murine interleukin-6 Biochemistry 39 1942 1950 10684643 10.1021/bi991973i 1:CAS:528: DC%2BD3cXotlyiug%3D%3D (Pubitemid 30124001)
23. N Morjana R Tal 1998 Expression and equilibrium denaturation of cardiac troponin I: stabilization of a folding intermediate during denaturation by urea Biotechnol Appl Biochem 28 7 17 9693083 1:CAS:528:DyaK1cXlsVWru7k%3D (Pubitemid 28369900)
24. CN Pace 1990 Measuring and increasing protein stability Trends Biotechnol 8 93 98 1367432 10.1016/0167-7799(90)90146-O 1:CAS:528:DyaK3cXltFWks7k%3D (Pubitemid 20110456)
25. Pace CN, Shirley BA, Thomson JA (1989) Protein structure and function: a practical approach. In: Creighton TE (ed) IRL Press, Oxford, pp 311-330
26. PL Privalov 1996 Intermediate states in protein folding J Mol Biol 258 707 725 8637003 10.1006/jmbi.1996.0280 1:CAS:528:DyaK28XjtFOgtrg%3D (Pubitemid 26150874)
27. OB Ptitsyn 1987 Protein folding: hypothesis and experiments J Protein Chem 6 273 293 10.1007/BF00248050 1:CAS:528:DyaL1cXitFyl
28. Ptitsyn OB (1992) The molten globule state. In: Creighton TE (ed) Protein folding. Freeman WH and Company, New York, pp 243-300
29. OB Ptitsyn 1995 Molten globule and protein folding Adv Protein Chem 47 83 229 8561052 10.1016/S0065-3233(08)60546-X 1:CAS:528:DyaK28XlvFOgsg%3D%3D
30. SE Radford 2000 Protein folding: progress maid and promises ahead Trends Biochem Sci 25 611 617 11116188 10.1016/S0968-0004(00)01707-2 1:CAS:528:DC%2BD3cXoslKntr0%3D
31. JF Schildbach CR Rabinson RT Sauer 1995 Biophysical characterization of Tra Y protein from Escherichia coli F factor J Biol Chem 273 1329 1333 10.1074/jbc.273.3.1329
32. Sears DW, Beychok S (1973) Physical properties and techniques of protein chemistry. In: Leach SJ (ed) Academic Press, New York, pp 445-593
33. EH Strickland 1974 Aromatic contribution to CD spectra of proteins CRC Crit Rev Biochem 2 113 175 4591332 10.3109/10409237409105445 1:STN:280:DyaE2c%2Fpslynsw%3D%3D
34. O Tcherkasskaya OB Ptitsyn 1999 Molten globule versus variety of intermediates influence of anions on pH denatured apomyoglobin FEBS Lett 455 325 331 10437798 10.1016/S0014-5793(99)00792-9 1:CAS:528:DyaK1MXks1Oltrw%3D (Pubitemid 29333061)
35. JB Udgaonakr 2008 Multiple routes and structural heterogeneity in protein folding Annu Rev Biophys 37 489 510 10.1146/annurev.biophys.37.032807.125920
36. VN Uversky AS Karnoup D Segel S Seshadry S Doniach AL Fink 1998 Anion-induced folding of staphylococcal nuclease: characterization of multiple partially folded intermediates J Mol Biol 278 879 894 9614949 10.1006/jmbi.1998.1741 1:CAS:528:DyaK1cXjsV2gtL4%3D (Pubitemid 28224903)
37. VN Uversky AS Karnoup R Khurana DJ Segel S Doniach AL Fink 1999 Association of partially folded intermediates of staphylococcal nuclease induces structure and stability Protein Sci 8 161 173 10210194 10.1110/ps.8.1.161 1:CAS:528:DyaK1MXlsFeqsA%3D%3D (Pubitemid 29035529)