A34. Palchevskyy, S.S., Posokhov, Y.O., Olivier, B., Popot, J-L, Pucci, B. and Ladokhin, A. S. Chaperoning of membrane protein insertion into lipid bilayers by hemifluorinated surfactants: application to diphtheria toxin Biochemistry 45, in press (2006).

A33. Posokhov, Y.O. and Ladokhin, A. S. Lifetime Fluorescence Method for Determining Membrane Topology of Proteins, Analytical Biochem. 348, 87-93 (2006).

A32. Ladokhin, A. S. and Haigler, H. T. Reversible Transition between the Surface Trimer and Membrane-Inserted Monomer of Annexin 12. Biochemistry 44, 34042-3409 (2005).

A31. Patel, D. R., Isas, J. M., Ladokhin, A. S., Jao, C. C., Kim, Y. E., Kirsch, T., Langen. R. and Haigler, H. T. The Conserved Core Domains of Annexins A1, A2, A5, and B12 Can Be Divided into Two Groups with Different Ca²⁺ -Dependent Membrane-Binding Properties. Biochemistry 44, 2833-2844 (2005).

A30. Ladokhin, A. S., Legmann, R., Collier, R. J. & White, S. H. Reversible refolding of the diphtheria toxin T-domain on lipid membranes. Biochemistry 43, 7451-7458 (2004).

A29. Ladokhin, A. S. & White, S. H. Interfacial folding and membrane insertion of a designed helical peptide. Biochemistry 43, 5782-5791 (2004).

A28. Ladokhin, A. S., Isas, J. M., Haigler, H. T. & White, S. H. Determining the membrane topology of proteins: Insertion pathway of a transmembrane helix of annexin 12. Biochemistry 41, 13617-13626 (2002).

A27. Ladokhin, A. S. & White, S. H. Protein chemistry at membrane interfaces: Non-additivity of electrostatic and hydrophobic interactions. J. Mol. Biol. 309, 543–552 (2001).

A26. Ladokhin, A. S. & White, S. H. Alphas and taus of tryptophan fluorescence in membranes. Biophys. J. 81, 99055–99058 (2001).

A25. Ladokhin, A. S. & White, S. H. ‘Detergent-like’ permeabilization of anionic lipid vesicles by melittin. Biochim. et Biophys. Acta, 1514, 253–260 (2001).

A24. Ladokhin, A. S. On the interpretation of decay-associated fluorescence spectra in proteins. Biopolymers & Cell 17, 221–224 (2001).

A23. Ladokhin, A. S., Jayasinghe, S. & White, S. H. How to measure tryptophan fluorescence in membranes properly, and why bother? Analytical Biochem. 285, 235–245 (2000).

A22. Osapay, K., Tran, D., Ladokhin, A. S., White, S. H., Henschen, A. H. & Selsted, M. E. Formation and characterization of a single Trp-Trp crosslink in indolicidin that confers protease stability without altering antimicrobial activity. J. Biol. Chem. 275, 12017–12022 (2000).

A21. Ladokhin, A. S. Evaluation of lipid exposure of tryptophan residues in membrane peptides and proteins. Analytical Biochem. 276, 65–71 (1999).

A20. Ladokhin, A. S., Selsted, M. E. & White, S. H. CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix. Biochemistry 38, 12313–12319 (1999).

A19. Ladokhin, A. S. & White, S. H. Folding of amphipathic a -helices on membranes: Energetics of helix formation by melittin. J. Mol. Biol. 285, 1363–1369 (1999).

A18. Ladokhin, A. S. Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: Theoretical considerations. Biophys. J. 76, 946–955 (1999).

A17. Ladokhin, A. S. Red-edge excitation study of non-exponential fluorescence decay of indole in solution and in a protein. J. of Fluorescence 9, 1–10 (1999).

A16. Wimley, W. C., Hristova, K., Ladokhin, A. S., Silvestro, L., Axelsen, P. H. & White, S. H. Folding of b -sheet membrane proteins: A hydrophobic hexapeptide model. J. Mol. Biol. 277, 1091–1110 (1998).

A15. Ladokhin, A. S., Selsted, M. E. & White, S. H. Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: Pore formation by melittin. Biophys. J. 72, 1762–1766 (1997).

A14. Ladokhin, A. S., Selsted, M. E. & White, S. H. Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophys. J. 72, 794–805 (1997).

A13. Petrushenko, Z. M., Negrutskii, B. S., Ladokhin, A. S., Budkevich, T. V., Shalak, V. F. & El’skaya, A. V. Evidence for the formation of an unusual ternary complex of rabbit liver EF-1a with GDP and deacylated tRNA. FEBS Letters 407, 13–17 (1997).

A12. Ladokhin, A. S., Wimley, W. C. & White, S. H. Leakage of membrane vesicle contents: Determination of mechanism using fluorescence requenching. Biophys. J. 69, 1964–1971 (1995).

A11. Ladokhin, A. S. & Holloway, P. W. Fluorescence of membrane-bound tryptophan octyl ester. A model for studying intrinsic fluorescence of protein–membrane interactions. Biophys. J. 69, 506–517 (1995).

A10. Ladokhin, A. S. & Holloway, P. W. Fluorescence quenching study of melittin-membrane interactions. Ukrainian Biochem. J. 67, 34–40 (1995).

A9. Ladokhin, A. S. & Brand, L. Evidence for an excited-state reaction contributing to NADH fluorescence. J. of Fluorescence 5, 99–106 (1995).

A8. Ladokhin, A. S., Wang, L., Steggles, A. W., Malak, H. & Holloway, P. W. Fluorescence study of a temperature induced conversion from the "loose" to the "tight" binding form of membrane-bound cytochrome b5. Biochemistry 32, 6951–6956 (1993).

A7. Tretyachenko-Ladokhina, V. G., Ladokhin, A. S., Wang, L., Steggles, A. W. & Holloway, P. W. Amino acid substitutions in the membrane-binding domain of cytochrome b5 alter its membrane-binding properties. Biochim. et Biophys. Acta 1153, 163–169 (1993).

A6. Ladokhin, A. S., Holloway, P. W. & Kostrzhevska, E. G. Distribution analysis of membrane penetration by depth-dependent fluorescence quenching. J. of Fluorescence 3, 195–197 (1993).

A5. Ladokhin, A. S., Wang, L., Steggles, A. W. & Holloway, P. W. Fluorescence study of a mutant cytochrome b5 with a single tryptophan in the membrane binding domain. Biochemistry 30, 10200–10206 (1991).

A4. Demchenko A. P. & Ladokhin, A. S. Temperature-dependent shift of fluorescence spectra without conformational changes in protein: Studies of dipole relaxation in the melittin molecule. Biochim. et Biophys. Acta. 955, 352-360 (1988).

A3. Demchenko, A. P. & Ladokhin, A. S. Red-edge excitation fluorescence spectroscopy of indole and tryptophan. Eur. Biophys. J. 15, 369-379 (1988).

A2. Kamalov, V. F., Ladokhin, A. S. & Toleutaev, B. N. Intramolecular nanosecond dynamics of melittin. Proc. Acad. Sci. USSR 296, 742-745 (1987).

A1. Demchenko, A. P., Ladokhin, A. S., Kostrzevska, E. G. & Dibrova, T. L. Structural dynamics in the environment of the tryptophan residue in melittin. Molecular Biology 21, 553-560 (1987).

B7. London, E. & Ladokhin, A. S. Measuring the depth of amino acid residues in membrane-inserted peptides by fluorescence quenching. In Current Topics in Membranes: Peptide–Lipid Interactions (eds Simon, S. A. & McIntosh, T. J.) 52, 89-115 (Academic Press, New York., 2002).

B6. White, S. H., Ladokhin, A. S, Jayasinghe, S. & Hristova, K. How membranes shape protein structure. J. Biol. Chem. 276, 32395–32398 (2001). (minireview)

B5. Ladokhin, A. S. Fluorescence spectroscopy in peptide and protein analysis. In Encyclopedia of Analytical Chemistry: Instrumentation and Applications (ed Meyers, R. A.) 5762–5779 (Wiley, Chichester, 2000).

B4. White, S. H., Wimley, W. C., Ladokhin, A. S, & Hristova, K. Protein folding in membranes: Pondering the nature of the bilayer milieu. Biol. Skr. Dan. Selsk. 49, 99–106 (1998).

B3. White, S. H., Wimley, W. C., Ladokhin, A. S, & Hristova, K. Methods for determining the energetics of peptide–bilayer interactions. Methods in Enzymology 295, 62–87 (1998).

B2. Ladokhin, A. S., Wimley, W. C., Hristova, K., & White, S. H. Mechanism of leakage of contents of membrane vesicles determined by fluorescence requenching. Methods in Enzymology 278, 474–486 (1997).

B1. Ladokhin, A. S. Distribution analysis of depth-dependent fluorescence quenching in membranes: A practical guide. Methods in Enzymology 278, 462–473 (1997).