Slowtert-butyl ester acidolysis and peptide 310-helix to α-helix transition in HFIP solution
نویسندگان
چکیده
منابع مشابه
A theoretical study on quadrupole coupling parameters of HRPII Protein modeled as 310-helix & α-helix structures
A fragment of Histidine rich protein II (HRP II 215-236) was investigated by 14N and 17O electric field gradient, EFG, tensor calculations using DFT. This study is intended to explore the differences between 310-helix and α-helix of HRPII both in the gas phase and in solution. To achieve the aims, the 17O and 14N NQR parameters of a fragment of HRPII (215-236) for both structures are calculated...
متن کاملa theoretical study on quadrupole coupling parameters of hrpii protein modeled as 310-helix & α-helix structures
a fragment of histidine rich protein ii (hrp ii 215-236) was investigated by 14n and 17o electric field gradient, efg, tensor calculations using dft. this study is intended to explore the differences between 310-helix and α-helix of hrpii both in the gas phase and in solution. to achieve the aims, the 17o and 14n nqr parameters of a fragment of hrpii (215-236) for both structures are calculated...
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XAO peptide (Ac-X2A7O2-NH2; X: diaminobutyric acid side chain, -CH2CH2NH3(+); O: ornithine side chain, -CH2CH2CH2NH3(+)) in aqueous solution shows a predominantly polyproline II (PPII) conformation without any detectable α-helix-like conformations. Here we demonstrate by using circular dichroism (CD), ultraviolet resonance Raman (UVRR) and nuclear magnetic resonance (NMR) spectroscopy that sodi...
متن کاملThe role of [alpha]-, 310-, and [pi]-helix in helix[rarr]coil transitions
The conformational equilibrium between 310and -helical structure has been studied via high-resolution NMR spectroscopy by Millhauser and coworkers using the MW peptide Ac-AMAAKAWAAKA AAARA-NH2. Their 750-MHz nuclear Overhauser effect spectroscopy (NOESY) spectra were interpreted to reflect appreciable populations of 310-helix throughout the peptide, with the greatest contribution at the N and C...
متن کاملDirect UV Raman Monitoring of 310-Helix and π-Bulge Premelting during r-Helix Unfolding
We used UV resonance Raman (UVRR) spectroscopy exciting at ∼200 nm within the peptide bond π f π* transitions to selectively study the amide vibrations of peptide bonds during R-helix melting. The dependence of the amide frequencies on theirΨ Ramachandran angles and hydrogen bonding enables us, for the first time, to experimentally determine the temperature dependence of the peptide bond Ψ Rama...
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ژورنال
عنوان ژورنال: Biopolymers
سال: 2007
ISSN: 0006-3525,1097-0282
DOI: 10.1002/bip.20680