Literature DB >> 25447875

Insoluble protein assemblies characterized by fourier transform infrared spectroscopy.

Antonino Natalello1, Silvia M Doglia.   

Abstract

Fourier transform infrared (FTIR) spectroscopy is a useful tool for the structural characterization of insoluble protein assemblies, as it allows to obtain information on the protein secondary structures and on their intermolecular interactions. The protocols for FTIR spectroscopy and microspectroscopy measurements in transmission and attenuated total reflection modes will be presented and illustrated in the following examples: bacterial inclusion bodies, self-assembling peptides, thermal aggregates, and amyloid fibrils.

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Year:  2015        PMID: 25447875     DOI: 10.1007/978-1-4939-2205-5_20

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  11 in total

1.  Conformational Stability and Dynamics in Crystals Recapitulate Protein Behavior in Solution.

Authors:  Benedetta Maria Sala; Tanguy Le Marchand; Guido Pintacuda; Carlo Camilloni; Antonino Natalello; Stefano Ricagno
Journal:  Biophys J       Date:  2020-07-24       Impact factor: 4.033

2.  Methionine oxidation in α-synuclein inhibits its propensity for ordered secondary structure.

Authors:  Erika Ponzini; Antonella De Palma; Lucilla Cerboni; Antonino Natalello; Rossana Rossi; Rani Moons; Albert Konijnenberg; Joanna Narkiewicz; Giuseppe Legname; Frank Sobott; PierLuigi Mauri; Carlo Santambrogio; Rita Grandori
Journal:  J Biol Chem       Date:  2019-02-12       Impact factor: 5.157

3.  Characterization of the Conformational Properties of Soluble and Insoluble Proteins by Fourier Transform Infrared Spectroscopy.

Authors:  Diletta Ami; Antonino Natalello
Journal:  Methods Mol Biol       Date:  2022

4.  The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.

Authors:  Susanna Navarro; Patrizia Marinelli; Marta Diaz-Caballero; Salvador Ventura
Journal:  Microb Cell Fact       Date:  2015-07-11       Impact factor: 5.328

5.  Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure.

Authors:  Patrizia Marinelli; Irantzu Pallares; Susanna Navarro; Salvador Ventura
Journal:  Sci Rep       Date:  2016-10-06       Impact factor: 4.379

6.  Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence.

Authors:  Clara Iannuzzi; Margherita Borriello; Marianna Portaccio; Gaetano Irace; Ivana Sirangelo
Journal:  Int J Mol Sci       Date:  2017-11-28       Impact factor: 5.923

7.  Exploring the use of leucine zippers for the generation of a new class of inclusion bodies for pharma and biotechnological applications.

Authors:  Ramon Roca-Pinilla; Sara Fortuna; Antonino Natalello; Alejandro Sánchez-Chardi; Diletta Ami; Anna Arís; Elena Garcia-Fruitós
Journal:  Microb Cell Fact       Date:  2020-09-04       Impact factor: 5.328

8.  Modulating Kinetics of the Amyloid-Like Aggregation of S. aureus Phenol-Soluble Modulins by Changes in pH.

Authors:  Masihuz Zaman; Maria Andreasen
Journal:  Microorganisms       Date:  2021-01-07

9.  Pathological ATX3 Expression Induces Cell Perturbations in E. coli as Revealed by Biochemical and Biophysical Investigations.

Authors:  Diletta Ami; Barbara Sciandrone; Paolo Mereghetti; Jacopo Falvo; Tiziano Catelani; Cristina Visentin; Paolo Tortora; Salvador Ventura; Antonino Natalello; Maria Elena Regonesi
Journal:  Int J Mol Sci       Date:  2021-01-19       Impact factor: 5.923

10.  In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study.

Authors:  Diletta Ami; Francesca Lavatelli; Paola Rognoni; Giovanni Palladini; Sara Raimondi; Sofia Giorgetti; Luca Monti; Silvia Maria Doglia; Antonino Natalello; Giampaolo Merlini
Journal:  Sci Rep       Date:  2016-07-04       Impact factor: 4.379

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