Reference

Solid-Phase Synthesis and CD Spectroscopic Investigations of Novel b-Peptides from L-Aspartic Acid and b-Amino-L-alanine

All Rights Reserved.Some chemicals with cas registry numbers like 144120-53-6 and 28920-43-6 are also used. Solid-Phase Synthesis and CD Spectroscopic Investigations of Novel b-Peptides from L-Aspartic Acid and b-Amino-L-alanine. Ahmed, Sahar; Beleid, Reem; Sprules, Tara; Kaur, Kamaljit (Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, AB T6G 2N8, Can.). Organic Letters, 9(1), 25-28 (English) 2007 American Chemical Society. CODEN: ORLEF7. ISSN: 1523-7060. DOCUMENT TYPE: Journal CA Section: 34 (Amino Acids, Peptides, and Proteins) Section cross-reference(s): 22 A solid-phase synthesis method for the prepn. of novel b3- and b2-peptides derived from L-aspartic acid and b-amino-L-alanine, resp., is described. The methodol. allows independent buildup of the b-peptide backbone and the introduction of sequential side chain substitutions. Representative peptides from the two classes, an amino-substituted b3-hexapeptide and an acyl-substituted b2-hexapeptide, have been prepd., and their soln. conformation is studied by CD spectroscopy. .

Rapid photochemical triggering of protein unfolding in a nondenaturing environment

Rapid photochemical triggering of protein unfolding in a nondenaturing environment. Rock, Ronald S.; Hansen, Kirk C.; Larsen, Randy W.; Chan, Sunney I. ( Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125, USA). Chemical Physics, 307(2-3), 201-208 (English) 2004 Elsevier B.V. CODEN: CMPHC2. ISSN: 0301-0104. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) Section cross-reference(s): 6 A general, rapid method for triggering protein unfolding is demonstrated using the photolabile protecting group 3',5'-dimethoxybenzoin (DMB). This protecting group is introduced in a site-specific manner to block a mutation known to destabilize the GCN4-p1 coiled-coil. Upon photolysis, the unfavorable interaction is unmasked and the peptide unfolds, as seen in the decrease in a-helical ellipticity. 120-14-9 and 144120-53-6 are cas registry numbers of chemicals which are used as reagents here. Photothermal beam deflection and photoacoustic calorimetry reveal kinetic processes and assocd. vol. changes with rates of 2′105-3′106 s-1, demonstrating that this photochem. technique is capable of triggering rapid protein conformational changes. Furthermore, this system allows conformational triggering under native solvent conditions, in the absence of chem. denaturants. The application of this strategy to following the early kinetics events in protein folding is discussed. .