Nanosecond T-jump experiment in poly(glutamic acid): A circular dichroism study

International Journal of Molecular Sciences

Volumn 13, Issue 2, 2012, Pages 2239-2248

  Mendonça, Lucille ^a   Hache, François ^a  

^a LABORATOIRE D OPTIQUE ET BIOSCIENCES   (France)

Author keywords

Circular dichroism; Poly(glutamic acid); T jump

Indexed keywords

POLYGLUTAMIC ACID; ALUMINUM OXIDE; GLUTAMIC ACID; POLYMERS; TITANIUM;

ABSORPTION SPECTROSCOPY; ACCURACY; ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; EXPERIMENTAL STUDY; FRACTIONATION; INTERMETHOD COMPARISON; MOLECULAR DYNAMICS; MOLECULAR EVOLUTION; MOLECULAR WEIGHT; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; PROTEIN UNFOLDING; STEADY STATE; TEMPERATURE DEPENDENCE; TEMPERATURE SENSITIVITY; CHEMISTRY; KINETICS; LASERS; METHODS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE;

ALUMINUM OXIDE; CIRCULAR DICHROISM; GLUTAMIC ACID; KINETICS; LASERS; POLYMERS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; TITANIUM;

EID: 84857666546     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms13022239     Document Type: Article

References (20)

1. Fersht, A.R. From the first protein structures to our current knowledge of protein folding: Delights and scepticisms. Nat. Rev. Mol. Cell Biol. 2008, 9, 650-654.
2. Dill, K.A.; Ozkan, S.B.; Shell, M.S.; Weikl, T.R. The protein folding problem. Annu. Rev. Biophys. 2008, 37, 289-316.
3. Krieger, F.; Fierz, B.; Bieri, O.; Drewello, M.; Kiefhaber, T. Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding. J. Mol. Biol. 2003, 332, 265-274.
4. Eaton, W.A.; Muñoz, V.; Thompson, P.A.; Henry, E.R.; Hofrichter, J. Kinetics and dynamics of loops, a-helices, b-hairpins and fast-folding proteins. Acc. Chem. Res. 1998, 31, 745-753.
5. Marquese, S.; Robbins, V.H.; Baldwin, R.L. Unusually stable helix formation in short alanine-based peptides. Biochemistry 1989, 86, 5286-5290.
6. Kimura, T.; Takahashi, S.; Akiyama, S.; Uzawa, T.; Ishimori, K.; Morishima, I. Direct observation of the multistep helix formation of poly-L-glutamic acid. J. Am. Chem. Soc. 2002, 124, 11596-11597.
7. Callender, R.H.; Dyer, R.B. Probing protein dynamics using temperature jump relaxation spectroscopy. Curr. Opin. Struct. Biol. 2002, 12, 628-633.
8. Pozo Ramajo, A.; Petty, S.A.; Starzyk, A.; Decatur, A.M.; Volk, M. The α-helix folds more rapidly at the C-terminus than at the N-terminus. J. Am. Chem. Soc. 2005, 127, 13784-13785.
9. Wang, T.; Du, D.; Gai, F. Helix-coil kinetics of two 14-residue peptides. Chem. Phys. Lett. 2003, 370, 842-848.
10. Shashilov, V.A.; Sikirzhytski, V.; Popova, L.A.; Lednev, I.K. Quantitative methods for structural characterization of proteins based on deep UV resonance Raman spectroscopy. Methods 2010, 52, 23-37.
11. Fasman, G.D. Circular Dichroism and the Conformational Analysis of Biomolecules; Plenum Press: New York, NY, USA, 1996.
12. Wallace, B.A.; Janes, R.W. Synchrotron radiation circular dichroism spectroscopy of proteins: Secondary structure, fold recognition and structural genomics. Curr. Opin. Chem. Biol. 2001, 5, 567-571.
13. Rohl, C.A.; Baldwin, R.L. Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-Coil transition in peptides. Biochemistry 1997, 36, 8435-8442.
14. Jennings, B.R.; Spach, G.; Schuster, T.M. Specific aggregation of poly(α-L-Glutamic acid) and hysteresis effects in aqueous solutions. I. Influence of temperature-dependent aggregation on the optical rotation of PGA. Biopolymers 1968, 6, 635-652.
15. Krejtschi, C.; Hauser, K. Stability and folding dynamics of polyglutamic acid. Eur. Biophys. J. 2011, 40, 673-685.
16. Rosenheck, K.; Doty, P. The far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on conformation. Proc. Natl. Acad. Sci. USA 1961, 47, 1775-1785.
17. Lednev, I.K.; Karnoup, A.S.; Sparrow, M.C.; Asher, S.A. α-helix peptide folding and unfolding activation barriers: A nanosecond UV resonance Raman study. J. Am. Chem. Soc. 1999, 121, 8074-8086.
18. Sharma, S. Helix-Coil Transition Dynamics of -Helical Peptides. PhD thesis, University of Liverpool, Liverpool, UK, 12 October 2006.
19. Khuc, M.T.; Mendonça, L.; Sharma, S.; Solinas, X.; Volk, M.; Hache, F. Measurement of circular dichroism dynamics in a nanosecond temperature-jump experiment. Rev. Sci. Instrum. 2011, 82, 054302:1-054302:8.
20. Wen, Y.X.; Chen, E.; Lewis, J.W.; Kliger, D.S. Nanosecond time-resolved circular dichroism measurements using an upconverted Ti:sapphire laser. Rev. Sci. Instrum. 1996, 67, 3010-3016.