Dynamic single-molecule force spectroscopy of rhodopsin in native membranes

Methods in Molecular Biology

Volumn 1271, Issue , 2015, Pages 173-185

  Park, Paul S H ^a   Müller, Daniel J ^a  

^a NONE

Author keywords

Atomic force microscopy; Biological membranes; Energy landscape; Intramolecular interactions; Membrane proteins; Protein stability; Protein unfolding

Indexed keywords

G PROTEIN COUPLED RECEPTOR; MEMBRANE PROTEIN; RHODOPSIN;

ARTICLE; ATOMIC FORCE MICROSCOPY; DYNAMIC SINGLE MOLECULE FORCE SPECTROSCOPY; LIPID BILAYER; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; SPECTROSCOPY;

EID: 84923698202     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2330-4_12     Document Type: Article

References (30)

1. Müller DJ (2008) AFM: a nanotool in membrane biology. Biochemistry 47:7986–7998
2. Whited AM, Park PS (2014) Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands. Biochim Biophys Acta 1838:56–68
3. Kedrov A, Janovjak H, Sapra KT et al (2007) Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu Rev Biophys Biomol Struct 36:233–260
4. Papermaster DS, Dreyer WJ (1974) Rhodopsin content in the outer segment membranes of bovine and frog retinal rods. Biochemistry 13:2438–2444
5. Sapra KT, Park PS, Filipek S et al (2006) Detecting molecular interactions that stabilize native bovine rhodopsin. J Mol Biol 358:255–269
6. Park PS, Sapra KT, Kolinski M et al (2007) Stabilizing effect of Zn2+ in native bovine rhodopsin. J Biol Chem 282:11377–11385
7. Park PS, Sapra KT, Jastrzebska B et al (2009) Modulation of molecular interactions and function by rhodopsin palmitylation. Biochemistry 48:4294–4304
8. Evans E (2001) Probing the relation between force–lifetime–and chemistry in single molecular bonds. Annu Rev Biophys Biomol Struct 30:105–128
9. Sapra KT, Park PS, Palczewski K et al (2008) Mechanical properties of bovine rhodopsin and bacteriorhodopsin: possible roles in folding and function. Langmuir 24:1330–1337
10. Kawamura S, Colozo AT, Müller DJ et al (2010) Conservation of molecular interactions stabilizing bovine and mouse rhodopsin. Biochemistry 49:10412–10420
11. Mendes HF, van der Spuy J, Chapple JP et al (2005) Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy. Trends Mol Med 11:177–185
12. Sieving PA, Richards JE, Naarendorp F et al (1995) Dark-light: model for nightblindness from the human rhodopsin Gly-90 –> Asp mutation. Proc Natl Acad Sci U S A 92:880–884
13. Kawamura S, Colozo AT, Ge L et al (2012) Structural, energetic, and mechanical perturbations in rhodopsin mutant that causes congenital stationary night blindness. J Biol Chem 287:21826–21835
14. Kawamura S, Gerstung M, Colozo AT et al (2013) Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin. Structure 21:426–437
15. Zocher M, Fung JJ, Kobilka BK et al (2012) Ligandspecific interactions modulate kinetic, energetic, and mechanical properties of the human beta2 adrenergic receptor. Structure 20:1391–1402
16. Müller DJ, Engel A (2007) Atomic force microscopy and spectroscopy of native membrane proteins. Nat Protoc 2:2191–2197
17. Fotiadis D, Müller DJ (2013) High-resolution imaging of 2D outer membrane protein F crystals by atomic force microscopy. Methods Mol Biol 955:461–474
18. Sapra KT (2013) Atomic force microscopy and spectroscopy to probe single membrane proteins in lipid bilayers. Methods Mol Biol 974:73–110
19. Butt H-J, Jaschke M (1995) Calculation of thermal noise in atomic force microscopy. Nanotechnology 6:1–7
20. Bustamante C, Marko JF, Siggia ED et al (1994) Entropic elasticity of lambda-phage DNA. Science 265:1599–1600
21. Evans E (1999) Looking inside molecular bonds at biological interfaces with dynamic force spectroscopy. Biophys Chem 82:83–97
22. Molday RS, Hicks D, Molday L (1987) Peripherin. A rim-specific membrane protein of rod outer segment discs. Invest Ophthalmol Vis Sci 28:50–61
23. Bosshart PD, Casagrande F, Frederix PL et al (2008) High-throughput single-molecule force spectroscopy for membrane proteins. Nanotechnology 19:384014
24. Bosshart PD, Frederix PL, Engel A (2012) Reference-free alignment and sorting of single-molecule force spectroscopy data. Biophys J 102:2202–2211
25. Struckmeier J, Wahl R, Leuschner M et al (2008) Fully automated single-molecule force spectroscopy for screening applications. Nanotechnology 19:384020
26. Rief M, Gautel M, Oesterhelt F et al (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276:1109–1112
27. Müller DJ, Kessler M, Oesterhelt F et al (2002) Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys J 83:3578–3588
28. Dietz H, Rief M (2004) Exploring the energy landscape of GFP by single-molecule mechanical experiments. Proc Natl Acad Sci U S A 101:16192–16197
29. Bieri O, Wirz J, Hellrung B et al (1999) The speed limit for protein folding measured by triplet-triplet energy transfer. Proc Natl Acad Sci U S A 96:9597–9601
30. Howard J (2001) Mechanics of motor proteins and the cytoskeleton. Sinauer Associates, Inc., Sunderland, MA