Literature DB >> 24134469

Distribution of protein Ramachandran psi (ψ) angle using non-resonance visible raman scattering measurements.

Susmita Bhattacharya1, Sudeshna Ghosh, Nitin Kumar Pandey, Susmitnarayan Chaudhury, Swagata Dasgupta, Anushree Roy.   

Abstract

Knowing the distribution of Ramachandran angles helps in understanding peptide and protein backbone conformation. Empirical relations are proposed to correlate the spectral profile of the amide III3 band, obtained from ultraviolet resonance Raman measurements (UVRR), with the Ramachandran dihedral psi angle distribution in small peptide and protein molecules, in different environmental conditions (Mikhonin et al. J. Phys. Chem. B 2006, 110, 1928-1943). It has also been used for more complicated structures, like large globular proteins and protein fibrils. In our work here, we use visible Raman spectra and available empirical relations to obtain similar correlations for human serum albumin, hen egg white lysozyme, and human gamma crystallin. We also report the dihedral angle distribution in fibrils and a denatured protein in an ethanol environment using the same spectroscopic technique.

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Year:  2013        PMID: 24134469     DOI: 10.1021/jp408009y

Source DB:  PubMed          Journal:  J Phys Chem B        ISSN: 1520-5207            Impact factor:   2.991


  2 in total

1.  Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies.

Authors:  Alexey V Krasnoslobodtsev; Tanja Deckert-Gaudig; Yuliang Zhang; Volker Deckert; Yuri L Lyubchenko
Journal:  Ultramicroscopy       Date:  2016-03-30       Impact factor: 2.689

2.  Nicking and fragmentation are responsible for α-lactalbumin amyloid fibril formation at acidic pH and elevated temperature.

Authors:  Rajesh Mishra
Journal:  Protein Sci       Date:  2021-06-17       Impact factor: 6.993

  2 in total

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