Raman Optical Activity of the Central Part of Hinge Peptide

Autor:	Marie Urbanová, Vladimír Baumruk, Josef Kapitán, Erich Wünsch, Vladimír Gut, Jan Hlaváček, Petr Maloň, Helena Dlouhá
Rok vydání:	2005
Předmět:	chemistry.chemical_classification Stereochemistry Dimer Hinge Peptide General Chemistry Pentapeptide repeat symbols.namesake Crystallography chemistry.chemical_compound chemistry Vibrational circular dichroism symbols Raman optical activity Raman spectroscopy Polyproline helix
Zdroj:	Collection of Czechoslovak Chemical Communications. 70:403-409
ISSN:	1212-6950 0010-0765
DOI:	10.1135/cccc20050403
Popis:	Central cyclic part of the hinge peptide (a parallel dimer of the pentapeptide Boc-Cys-Pro-Pro-Cys-Pro-NHCH3 with two disulfide bonds) derived from the sequence of human IgG1 is a rather rigid structure having predominantly polyproline II helical conformation as shown by vibrational circular dichroism spectra. It exhibits significant Raman optical activity (ROA) signal due to vibrations associated with the disulfide bridges. We report positive ROA for the S-S stretching vibration at 510 cm-1 and for the C-S stretching vibration at 655 cm-1. These signals can provide means to assess the conformation of disulfide bridges in proteins, otherwise difficult to investigate.
Databáze:	OpenAIRE
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