Measuring membrane protein stability under native conditions

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 1, 2014, Pages 219-224

  Chang, Yu Chu ^a   Bowie, James U ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Membrane protein folding; Steric trap

Indexed keywords

BACTERIORHODOPSIN; DIMYRISTOYLPHOSPHATIDYLCHOLINE; MEMBRANE PROTEIN;

ARTICLE; ENERGY YIELD; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STABILITY; PROTEIN UNFOLDING; STERIC TRAPPING; THERMOSTABILITY;

MEMBRANE PROTEIN FOLDING; STERIC TRAP;

BACTERIORHODOPSINS; BIOTIN; BIOTINYLATION; DIMYRISTOYLPHOSPHATIDYLCHOLINE; HALOBACTERIUM SALINARUM; KINETICS; LIPID BILAYERS; MEMBRANE PROTEINS; MICELLES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE; THERMODYNAMICS;

EID: 84891917719     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1318576111     Document Type: Article

References (23)

1. Fersht A (1999) Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding (Freeman, New York).
2. Pace CNC (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131: 266-280.
3. 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(20): 6795-6804.
4. Jackson SE (1998) How do small single-domain proteins fold? Fold Des 3(4):R81-R91.
5. Braiman MS, Stern LJ, Chao BH, Khorana HG (1987) Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli. J Biol Chem 262(19): 9271-9276.
6. Booth PJP, et al. (1995) Intermediates in the folding of the membrane protein bacteriorhodopsin. Nat Struct Biol 2(2): 139-143.
7. Curnow P, Booth PJ (2007) Combined kinetic and thermodynamic analysis of alphahelical membrane protein unfolding. Proc Natl Acad Sci USA 104(48): 18970-18975.
8. Booth PJ, Clarke J (2010) Membrane protein folding makes the transition. Proc Natl Acad Sci USA 107(9): 3947-3948.
9. Lau FW, Bowie JU (1997) A method for assessing the stability of a membrane protein. Biochemistry 36(19): 5884-5892.
10. Cao Z, Schlebach JP, Park C, Bowie JU (2012) Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state. Biochim Biophys Acta 1818: 1049-1054.
11. Chen GQ, Gouaux E (1999) Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: Evaluation of reversible unfolding conditions. Biochemistry 38(46): 15380-15387.
12. Schlebach JP, Cao Z, Bowie JU, Park C (2012) Revisiting the folding kinetics of bacteriorhodopsin. Protein Sci 21(1): 97-106.
13. Faham S, et al. (2004) Side-chain contributions to membrane protein structure and stability. J Mol Biol 335(1): 297-305.
14. Blois TM, Hong H, Kim TH, Bowie JU (2009) Protein unfolding with a steric trap. J Am Chem Soc 131(39): 13914-13915.
15. Hong H, Blois TM, Cao Z, Bowie JU (2010) Method to measure strong protein-protein interactions in lipid bilayers using a steric trap. Proc Natl Acad Sci USA 107(46): 19802-19807.
16. Hong H, Bowie JU (2011) Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments. J Am Chem Soc 133(29): 11389-11398.
17. Bayer EAE, Ehrlich-Rogozinski SS, Wilchek MM (1996) Sodium dodecyl sulfatepolyacrylamide gel electrophoretic method for assessing the quaternary state and comparative thermostability of avidin and streptavidin. Electrophoresis 17(8): 1319-1324.
18. Schlebach JP, Kim M-S, Joh NH, Bowie JU, Park C (2011) Probing membrane protein unfolding with pulse proteolysis. J Mol Biol 406(4): 545-551.
19. McKibbin C, et al. (2007) Opsin stability and folding: Modulation by phospholipid bicelles. J Mol Biol 374(5): 1319-1332.
20. Broecker J, Keller S (2013) Impact of urea on detergent micelle properties. Langmuir 29(27): 8502-8510.
21. Gerrits M, et al. (2007) Cell-Free Synthesis of Defined Protein Conjugates by Site-Directed Cotranslational Labeling, eds Katzen F, Bennett R, KudlickiW(Landes Bioscience, Austin, TX), pp 166-180.
22. Oesterhelt D, Stoeckenius W (1974) Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol 31: 667-678.
23. Howarth M, et al. (2006) A monovalent streptavidin with a single femtomolar biotin binding site. Nat Methods 3(4): 267-273.