Vacuum-ultraviolet circular dichroism analysis of biomolecules

Chirality

Volumn 18, Issue 5, 2006, Pages 329-334

  Gekko, Kunihiko ^a   Matsuo, Koichi ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Amino acids; Proteins; Saccharides; Secondary structures; Synchrotron radiation; Theoretical analysis

Indexed keywords

AMINO ACID; CARBOHYDRATE; GLOBULAR PROTEIN; HYDROXYL GROUP; PROTEIN;

AB INITIO CALCULATION; AQUEOUS SOLUTION; CIRCULAR DICHROISM; CONFERENCE PAPER; DENSITY FUNCTIONAL THEORY; ENERGY TRANSFER; PRIORITY JOURNAL; SPECTROPHOTOMETRY; SPECTROSCOPY; SYNCHROTRON RADIATION; ULTRAVIOLET RADIATION; VACUUM;

AMINO ACIDS; CARBOHYDRATES; CIRCULAR DICHROISM; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; SYNCHROTRONS; VACUUM;

EID: 33646346846     PISSN: 08990042     EISSN: 1520636X     Source Type: Journal    
DOI: 10.1002/chir.20252     Document Type: Conference Paper

References (19)

1. Fasman, GD. Circular dichroism and the conformational analysis of biomolecules. New York, NY: Plenum;1996.
2. Berova N, Nakanishi K, Woody RW. Circular dichroism: principles and applications, 2nd ed. New York, NY: Wiley-VCH;2000.
3. Johnson WC Jr. The circular dichroism of carbohydrates. Adv Carbohydr Chem Biochem 1987;45:73-124.
4. Snyder PA, Rowe EM. The first use of synchrotron radiation for vacuum ultraviolet circular dichroism measurements. Nucl Instrum Methods 1980;172:345-349.
5. Sutherland JC, Emrick A, France LL. Monteleone DC, Trunk J. Circular dichroism user facility at the National Synchrotron Light Source: estimation of protein secondary structure. Biotechniques 1992;13:588-590.
6. Wallace BA, Janes RW. Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics. Curr Opin Chem Biol 2001;5:567-571.
7. Ojima N, Sakai K, Fukazawa T, Gekko K. Vacuum-ultraviolet circular dichroism spectrophotometer using synchrotron radiation: optical system and off-line performance. Chem Lett 2000;29:832-833.
8. Ojima N, Sakai K, Matsuo K, Matsui T, Fukazawa T, Namatame H, Taniguchi M, Gekko K. Vacuum-ultraviolet circular dichroism spectrophotometer using synchrotron radiation: optical system and online performance. Chem Lett 2001;30:522-523.
9. Matsuo K, Sakai K, Matsushima Y, Fukuyama T, Gekko K. Optical cell with a temperature-control unit for a vacuum-ultraviolet circular dichroism spectrophotometer. Anal Sci 2003;19:129-132.
10. Matsuo K, Matsushima Y, Fukuyama T, Senba S, Gekko K. Vacuum-ultraviolet circular dichroism of amino acids as revealed by synchrotron radiation spectrophotometer. Chem Lett 2002;31:826-827.
11. Fukuyama T, Matsuo K, Gekko K. Vacuum-ultraviolet electronic circular dichroism of L-alanine in aqueous solution investigated by time-dependent density functional theory. J Phys Chem A 2005a;109:6928-6933.
12. Bauernschmitt R, Ahlrichs R. Treatment of electronic excitations within the adiabatic approximation of time dependent density functional theory. Chem Phys Lett 1996;256:454-464.
13. Inagaki T. Optical absorptions of aliphatic amino acids in the far ultraviolet. Biopolymers 1973;12:1353-1362.
14. Matsuo K, Gekko K. Vacuum-ultraviolet circular dichroism study of saccharides by synchrotron radiation spectrophotometry. Carbohydr Res 2004a;339:591-597.
15. Matsuo K, Yonehara R, Gekko K. Secondary-structure analysis of proteins by vacuum-ultraviolet circular dichroism spectroscopy. J Biochem (Tokyo) 2004b;135:405-411.
16. Matsuo K, Yonehara R, Gekko K. Improved estimation of the secondary structures of proteins by vacuum-ultraviolet circular dichroism spectroscopy. J Biochem (Tokyo) 2005b;138:79-88.
17. Sreerama N, Woody RW. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 2000;287:252-260.
18. Jones GR, Clarke DT. Applications of extended ultra-violet circular dichroism spectroscopy in biology and medicine. Faraday Discuss 2004;126:223-236.
19. Sreerama N, Venyaminov SY, Woody RW. Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Sci 1999;8:370-380.