Robust and convenient analysis of protein thermal and chemical stability

Protein Science

Volumn 24, Issue 12, 2015, Pages 2055-2062

  Niklasson, Markus ^a   Andresen, Cecilia ^a   Helander, Sara ^a   Roth, Marie G L ^a   Zimdahl Kahlin, Anna ^a   Lindqvist Appell, Malin ^a   Lundström, Patrik ^a  

^a LINKÖPING UNIVERSITY   (Sweden)

Author keywords

chemical denaturation; circular dichroism; curve fitting; fluorescence; protein denaturation software; protein stability; protein stability software; thermal denaturation

Indexed keywords

BOVINE SERUM ALBUMIN; CALCIUM DEPENDENT PROTEIN KINASE 3; FATTY ACID BINDING PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; METHYLTRANSFERASE; PROTEIN KINASE C; THIOPURINE METHYL TRANSFERASE; UNCLASSIFIED DRUG; PROTEIN;

ANT; BINOCULAR CONVERGENCE; CATAGLYPHIS FORTIS; CHEMICAL DENATURATION; CIRCULAR DICHROISM; COMPARATIVE STUDY; COMPUTER INTERFACE; COMPUTER PROGRAM; CONTROLLED STUDY; CURVE FITTING; EQUILIBRIUM CONSTANT; FLUORESCENCE SPECTROSCOPY; FORMICA; FORMICA EXSECTA; HUMAN; NONHUMAN; ORYCTOLAGUS CUNICULIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN STABILITY; RABBIT; REVIEW; THERMODYNAMICS; THERMOSTABILITY; BIOLOGY; CHEMISTRY; MOLECULAR MODEL; PROCEDURES; SOFTWARE; SPECTROFLUOROMETRY; TEMPERATURE;

CIRCULAR DICHROISM; COMPUTATIONAL BIOLOGY; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEINS; SOFTWARE; SPECTROMETRY, FLUORESCENCE; TEMPERATURE;

EID: 84957605102     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2809     Document Type: Review

References (20)

1. Greenfield N, Fasman GD, (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8: 4108-4116.
2. Harder ME, Deinzer ML, Leid ME, Schimerlik MI, (2004) Global analysis of three-state protein unfolding data. Protein Sci 13: 2207-2222.
3. Levenberg K, (1944) A method for the solution of certain non-linear problems in least squares. Q J Appl Math 2: 164-168.
4. Marquardt DW, (1963) An algorithm for least-squared estimation of nonlinear parameters. J Soc Indus Appl Math 11: 431-441.
5. Mosteller F, Tukey JW (, 1977) Data analysis and regression. Reading, MA: Addison-Wesley Publishing Company.
6. Rees DC, Robertson AD, (2001) Some thermodynamic implications for the thermostability of proteins. Protein Sci 10: 1187-1194.
7. Myers JK, Pace CN, Scholtz JM, (1996) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci 5: 981-981.
8. Li JL, Baker DA, Cox LS, (2000) Sexual stage-specific expression of a third calcium-dependent protein kinase from Plasmodium falciparum. Biochim Biophys Acta Gene Struct Express 1491: 341-349.
9. Woodson LC, Weinshilboum RM, (1983) Human kidney thiopurine methyltransferase-purification and biochemical properties. Biochem Pharmacol 32: 819-826.
10. Wennerstrand P, Dametto P, Hennig J, Klingstedt T, Skoglund K, Appell ML, Martensson LG, (2012) Structural characteristics determine the cause of the low enzyme activity of two thiopurine S-methyltransferase allelic variants: a biophysical characterization of TPMT2 and TPMT5. Biochemistry 51: 5912-5920.
11. Furuhashi M, Hotamisligil GS, (2008) Fatty acid-binding proteins: role in metabolic diseases and potential as drug targets. Nat Rev Drug Discov 7: 489-503.
12. De Sancho D, Munoz V, (2011) Integrated prediction of protein folding and unfolding rates from only size and structural class. Phys Chem Chem Phys 13: 17030-17043.
13. Greenfield NJ, (2006) Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat Protoc 1: 2527-2535.
14. Lumry R, Eyring H, (1954) Conformation changes of proteins. J Phys Chem 58: 110-120.
15. Robertson AD, Murphy KP, (1997) Protein structure and the energetics of protein stability. Chem Rev 97: 1251-1267.
16. Privalov PL, (1979) Stability of proteins: small globular proteins. Adv Protein Chem 33: 167-241.
17. Becktel WJ, Schellman JA, (1987) Protein stability curves. Biopolymers 26: 1859-1877.
18. Schellman JA, (1994) The thermodynamics of solvent exchange. Biopolymers 34: 1015-1026.
19. Johnson CM, Fersht AR, (1995) Protein stability as a function of denaturant concentration-the thermal-stability of barnase in the presence of urea. Biochemistry 34: 6795-6804.
20. John DM, Weeks KM, (2000) van't Hoff enthalpies without baselines. Protein Sci 9: 1416-1419.