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Your search keyword '"Gowers, Sally A.N."' showing total 2 results
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2 results on '"Gowers, Sally A.N."'

1. Observation of [beta]-sheet aggregation in a gas-phase tau-peptide dimer

Author

Vaden, Timothy D., Gowers, Sally A.N., and Snoek, Lavina C.

Subjects
Hydrogen bonding -- Analysis, Infrared spectroscopy -- Usage, Molecular beams -- Usage, Peptides -- Chemical properties, Peptides -- Structure, Ultraviolet spectroscopy -- Usage, Chemistry
Abstract

Infrared (IR)/ultraviolet (UV) hole-burning spectroscopy is used for examining the aggregation of the protected segment (Ac-VQIVYK-NHMe) in the NH stretch region in a cold molecular beam in order to characterize its structure and identify the noncovalent interactions responsible for aggregation and stabilization in amyloid peptides. The studies have shown that the tau-protein fragments form extended [beta]-strands that are combined in a [beta]-sheet through characteristic backbone hydrogen bonds, indicating that this secondary structure is very energetic and is readily formed in the gas phase.

Published
2009

2. Conformational preferences of an amyloidogenic peptide: IR spectroscopy of Ac-VQIVYK-NHMe

Author

Vaden, Timothy D., Gowers, Sally A.N., de Boer, Tjalling S.J.A., Steill, Jeffrey D., Oomens, Jos, and Snoek, Lavina C.

Subjects
Infrared spectroscopy -- Usage, Lysine -- Chemical properties, Peptides -- Structure, Peptides -- Chemical properties, Chemistry
Abstract

The inherent conformational preferences of the capped hexapeptide Ac-VQIVYK-NHMe are characterized in the gas phase by using infrared/ultraviolet (IR/UV) double-resonance spectroscopy. The studies have shown that in the protonated tau-peptide fragment, the lysine N[H.sub.3.sup.+] is bound to the peptide backbone and has altered the neutral [beta]-strand/[beta]-turn conformation into a random-coil-like structure.

Published
2008

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