Immobilization of proteins for single-molecule fluorescence resonance energy transfer measurements of conformation and dynamics

Methods in Molecular Biology

Volumn 896, Issue , 2012, Pages 3-20

  Choi, Ucheor B ^a   Weninger, Keith R ^b   Bowen, Mark E ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Encapsulation; FRET; Intrinsically disordered proteins; Reconstitution; Single molecule fluorescence; Vesicle

Indexed keywords

BOVINE SERUM ALBUMIN; IMMOBILIZED PROTEIN; MACROGOL DERIVATIVE; MEMBRANE PROTEIN; STREPTAVIDIN;

ANIMAL; ARTICLE; BIOTINYLATION; CATTLE; CHEMISTRY; FLUORESCENCE RESONANCE ENERGY TRANSFER; LIPID BILAYER; METABOLISM; METHODOLOGY; MICROSCOPY; PROTEIN CONFORMATION; SURFACE PROPERTY;

ANIMALS; BIOTINYLATION; CATTLE; FLUORESCENCE RESONANCE ENERGY TRANSFER; IMMOBILIZED PROTEINS; LIPID BILAYERS; MEMBRANE PROTEINS; MICROSCOPY; POLYETHYLENE GLYCOLS; PROTEIN CONFORMATION; SERUM ALBUMIN, BOVINE; STREPTAVIDIN; SURFACE PROPERTIES;

EID: 84865345067     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-3704-8_1     Document Type: Article

References (21)

1. Uversky VN, Dunker AK (2010) Understanding protein non-folding. Biochim Biophys Acta 1804(6):1231-1264
2. Mao AH et al (2010) Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc Natl Acad Sci USA 107(18):8183-8188
3. Muller-Spath S et al (2010) Charge interactions can dominate the dimensions of intrinsically disordered proteins. Proc Natl Acad Sci USA 107(33):14609-14614
4. Uversky VN (2002) What does it mean to be natively unfolded? Eur J Biochem 269(1):2-12
5. Boehr DD, Nussinov R,Wright PE (2009) The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol 5 (11):789-796
6. Flory JP (1969) Statistical mechanics of chain molecules. Interscience, New York, NY
7. Stryer L, Haugland RP (1967) Energy transfer: a spectroscopic ruler. Proc Natl Acad Sci USA 58(2):719-726
8. Chen H, Rhoades E (2008) Fluorescence characterization of denatured proteins. Curr Opin Struct Biol 18(4):516-524
9. Ferreon AC et al (2009) Interplay of alphasynuclein binding and conformational switching probed by single-molecule fluorescence. Proc Natl Acad Sci USA 106(14):5645-5650
10. Weninger K et al (2008) Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16(2):308-320
11. Kalinin S et al (2010) On the origin of broadening of single-molecule FRET efficiency distributions beyond shot noise limits. J Phys Chem B 114(18):6197-6206
12. Boukobza E, Sonnenfeld A, Haran G (2001) Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy. J Phys Chem B 105(48):12165-12170
13. Rasnik I, McKinney SA, Ha T (2005) Surfaces and orientations: much to FRET about? Acc Chem Res 38(7):542-548
14. HaTet al (1999) Ligand-induced conformational changes observed in single RNA molecules. Proc Natl Acad Sci USA 96(16):9077-9082
15. Graneli A et al (2006) Organized arrays of individual DNA molecules tethered to supported lipid bilayers. Langmuir 22(1):292-299
16. Roy R, Hohng S, Ha T (2008) A practical guide to single-molecule FRET. Nat Methods 5(6):507-516
17. Pertsinidis A, Zhang Y, Chu S (2010) Subnanometre single-molecule localization, registration and distance measurements. Nature 466 (7306):647-651
18. Lee NK et al (2005) Accurate FRET measurements within single diffusing biomolecules using alternating-laser excitation. Biophys J 88(4):2939-2953
19. McCann JJ et al (2010) Optimizing methods to recover absolute FRET efficiency from immobilized single molecules. Biophys J 99 (3):961-970
20. McKinney SA, Joo C, Ha T (2006) Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys J 91 (5):1941-1951
21. Sass LE et al (2010) Single-molecule FRET TACKLE reveals highly dynamic mismatched DNA-MutS complexes. Biochemistry 49 (14):3174-3190