2007
DOI: 10.1021/la702037k
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Structure and Orientation Changes of ω- and γ-Gliadins at the Air−Water Interface:  A PM−IRRAS Spectroscopy and Brewster Angle Microscopy Study

Abstract: Microscopic and molecular structures of ω-and γ-gliadin monolayers at the air-water interface were studied under compression by three complementary techniques: compression isotherms, polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS), and Brewster angle microscopy (BAM). For high molecular areas, gliadin films are homogeneous, and a flat orientation of secondary structures relative to the interface is observed. With increasing compression, the nature and orientation of secondary str… Show more

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Cited by 53 publications
(66 citation statements)
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“…Furthermore, a band around 1454 cm –1 is observed. This band can be assigned to CN vibrations in proline residues (2628) and is therefore consistent with the presence of 24 proline residues in MGD1 (~6%). At 20 h following protein injection, the intensity of amide I band slightly decreases and becomes more centered at 1635 cm –1 as assigned to β sheets.…”
Section: Resultssupporting
confidence: 83%
“…Furthermore, a band around 1454 cm –1 is observed. This band can be assigned to CN vibrations in proline residues (2628) and is therefore consistent with the presence of 24 proline residues in MGD1 (~6%). At 20 h following protein injection, the intensity of amide I band slightly decreases and becomes more centered at 1635 cm –1 as assigned to β sheets.…”
Section: Resultssupporting
confidence: 83%
“…IRRAS can be conducted at physiological temperature, at desired buffer and lipid compositions, and at low initial protein concentrations. IRRAS has previously been used to determine the orientation of short peptides in lipid monolayers (12-17), and secondary-structure changes of proteins upon ad- sorption to various interfaces (18)(19)(20)(21). Changes in the shape of IRRA bands were also used to postulate protein reorientations (22,23).…”
Section: Discussionmentioning
confidence: 99%
“…If the band appears as two components: one at the β-sheet position and another as a shoulder at 1682-1710 cm −1 it is indicative of an antiparallel β-sheet. The parallel β-sheet is predicted to have higher frequency for the lower component [62,64,65]. The disorder of random coils (unstructured) occurs at the same wavenumbers of the α-helices (1637-1650 cm −1 ), originating from the former broader and less intense bands compared to the α-helices [62,64,66].…”
Section: Pm-irrasmentioning
confidence: 99%