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388 related items for PubMed ID: 16787970
1. A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Lees JG, Miles AJ, Wien F, Wallace BA. Bioinformatics; 2006 Aug 15; 22(16):1955-62. PubMed ID: 16787970 [Abstract] [Full Text] [Related]
2. Bioinformatics analyses of circular dichroism protein reference databases. Janes RW. Bioinformatics; 2005 Dec 01; 21(23):4230-8. PubMed ID: 16188926 [Abstract] [Full Text] [Related]
3. Novel methods for secondary structure determination using low wavelength (VUV) circular dichroism spectroscopic data. Lees JG, Miles AJ, Janes RW, Wallace BA. BMC Bioinformatics; 2006 Nov 17; 7():507. PubMed ID: 17112372 [Abstract] [Full Text] [Related]
4. A reference dataset for circular dichroism spectroscopy tailored for the betagamma-crystallin lens proteins. Evans P, Bateman OA, Slingsby C, Wallace BA. Exp Eye Res; 2007 May 17; 84(5):1001-8. PubMed ID: 17400211 [Abstract] [Full Text] [Related]
5. Circular-dichroism and synchrotron-radiation circular-dichroism spectroscopy as tools to monitor protein structure in a lipid environment. Matsuo K, Gekko K. Methods Mol Biol; 2013 May 17; 974():151-76. PubMed ID: 23404276 [Abstract] [Full Text] [Related]
6. Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics. Miles AJ, Wallace BA. Chem Soc Rev; 2006 Jan 17; 35(1):39-51. PubMed ID: 16365641 [Abstract] [Full Text] [Related]
7. A reference dataset for the analyses of membrane protein secondary structures and transmembrane residues using circular dichroism spectroscopy. Abdul-Gader A, Miles AJ, Wallace BA. Bioinformatics; 2011 Jun 15; 27(12):1630-6. PubMed ID: 21505036 [Abstract] [Full Text] [Related]
13. Charge-transfer transitions in the vacuum-ultraviolet of protein circular dichroism spectra. Bulheller BM, Miles AJ, Wallace BA, Hirst JD. J Phys Chem B; 2008 Feb 14; 112(6):1866-74. PubMed ID: 18198861 [Abstract] [Full Text] [Related]
14. Chemometric tools for classification and elucidation of protein secondary structure from infrared and circular dichroism spectroscopic measurements. Navea S, Tauler R, Goormaghtigh E, de Juan A. Proteins; 2006 May 15; 63(3):527-41. PubMed ID: 16456850 [Abstract] [Full Text] [Related]
15. Circular dichroism and its use in protein-folding studies. Clarke DT. Methods Mol Biol; 2011 May 15; 752():59-72. PubMed ID: 21713631 [Abstract] [Full Text] [Related]
16. Synchrotron radiation circular dichroism (SRCD) spectroscopy: an enhanced method for examining protein conformations and protein interactions. Wallace BA, Janes RW. Biochem Soc Trans; 2010 Aug 15; 38(4):861-73. PubMed ID: 20658968 [Abstract] [Full Text] [Related]
17. Prediction of protein secondary structure from circular dichroism using theoretically derived spectra. Louis-Jeune C, Andrade-Navarro MA, Perez-Iratxeta C. Proteins; 2012 Feb 15; 80(2):374-81. PubMed ID: 22095872 [Abstract] [Full Text] [Related]