scholarly journals Extreme cross-peak 2D spectroscopy

2014 ◽  
Vol 111 (28) ◽  
pp. 10031-10032 ◽  
Author(s):  
G. D. Scholes
Keyword(s):  
Cross Peak

Two-dimensional IR spectroscopy reveals a hidden Fermi resonance band in the azido stretch spectrum of β-azidoalanine

2020 ◽  
Vol 22 (34) ◽  
pp. 19223-19229
Author(s):  
Jun Young Park ◽  
Hyeok-Jun Kwon ◽  
Saptarsi Mondal ◽  
Hogyu Han ◽  
Kyungwon Kwak ◽  
...  
Keyword(s):  
Ir Spectroscopy ◽  
Ir Spectrum ◽  
Resonance Peak ◽  
Cross Peak ◽  
Fermi Resonance ◽  
Two Dimensional ◽  
2D Ir ◽  
Resonance Band

The 2D-IR spectrum of Ala-N3 shows cross-peak, but cannot be identified clearly. The 1D slice spectra obtained from 2D-IR spectrum reveals the presence of hidden Fermi resonance peak.

SOLARIA: A Protocol for Automated Cross-Peak Assignment and Structure Calculation for Solid-State Magic-Angle Spinning NMR Spectroscopy

2005 ◽  
Vol 117 (38) ◽  
pp. 6307-6310 ◽  
Author(s):  
Michele Fossi ◽  
Federica Castellani ◽  
Michael Nilges ◽  
Hartmut Oschkinat ◽  
Barth-Jan van Rossum
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Magic Angle Spinning ◽  
Structure Calculation ◽  
Cross Peak ◽  
Magic Angle ◽  
Peak Assignment ◽  
Angle Spinning

Attenuation of Cross-Peak Intensities in QUIET-BIRD-NOESY Experiments

1999 ◽  
Vol 140 (1) ◽  
pp. 289-292 ◽  
Author(s):  
Brian Cutting ◽  
Geoffrey Bodenhausen
Keyword(s):  
Cross Peak

scholarly journals Analysis of amyloid-like secondary structure in the Cryab-R120G knock-in mouse model of hereditary cataracts by two-dimensional infrared spectroscopy

PLoS ONE ◽  
2021 ◽  
Vol 16 (9) ◽  
pp. e0257098
Author(s):  
Ariel M. Alperstein ◽  
Kathleen S. Molnar ◽  
Sidney S. Dicke ◽  
Kieran M. Farrell ◽  
Leah N. Makley ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Mouse Model ◽  
Mutant Mouse ◽  
Cross Peak ◽  
Two Dimensional ◽  
Wild Type ◽  
Age Related ◽  
Human Lenses ◽  
Αb Crystallin ◽  
2Dir Spectroscopy

αB-crystallin is a small heat shock protein that forms a heterooligomeric complex with αA-crystallin in the ocular lens. It is also widely distributed in tissues throughout the body and has been linked with neurodegenerative diseases such as Alzheimer’s, where it is associated with amyloid fibrils. Crystallins can form amorphous aggregates in cataracts as well as more structured amyloid-like fibrils. The arginine 120 to glycine (R120G) mutation in αB-crystallin (Cryab-R120G) results in high molecular weight crystallin protein aggregates and loss of the chaperone activity of the protein in vitro, and it is associated with human hereditary cataracts and myopathy. Characterizing the amorphous (unstructured) versus the highly ordered (amyloid fibril) nature of crystallin aggregates is important in understanding their role in disease and important to developing pharmacological treatments for cataracts. We investigated protein secondary structure in wild-type (WT) and Cryab-R120G knock-in mutant mouse lenses using two-dimensional infrared (2DIR) spectroscopy, which has been used to detect amyloid-like fibrils in human lenses and measure UV radiation-induced changes in porcine lenses. Our goal was to compare the aggregated proteins in this mouse lens model to human lenses and evaluate the protein structural relevance of the Cryab-R120G knock-in mouse model to general age-related cataract disease. In the 2DIR spectra, amide I diagonal peak frequencies were red-shifted to smaller wavenumbers in mutant mouse lenses as compared to WT mouse lenses, consistent with an increase in ordered secondary structure. The cross peak frequency and intensity indicated the presence of amyloid in the mutant mouse lenses. While the diagonal and cross peak changes in location and intensity from the 2DIR spectra indicated significant structural differences between the wild type and mutant mouse lenses, these differences were smaller than those found in human lenses; thus, the Cryab-R120G knock-in mouse lenses contain less amyloid-like secondary structure than human lenses. The results of the 2DIR spectroscopy study confirm the presence of amyloid-like secondary structure in Cryab-R120G knock-in mice with cataracts and support the use of this model to study age-related cataract.

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