scholarly journals Unravelling Secondary Structure Changes on Individual Anionic Polysaccharide Chains by Atomic Force Microscopy

2014 ◽  
Vol 53 (21) ◽  
pp. 5376-5379 ◽  
Author(s):  
Larissa Schefer ◽  
Jozef Adamcik ◽  
Raffaele Mezzenga
Keyword(s):  
Atomic Force Microscopy ◽  
Secondary Structure ◽  
Force Microscopy ◽  
Atomic Force ◽  
Structure Changes

scholarly journals Spectroscopic Investigations of Pentobarbital Interaction with Transthyretin

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Saqer M. Darwish ◽  
Jafar Ghithan ◽  
Musa M. Abuteir ◽  
Mariam Faroun ◽  
Mahmoud M. Abu-hadid
Keyword(s):  
Atomic Force Microscopy ◽  
Spectral Analysis ◽  
Fourier Transform ◽  
Secondary Structure ◽  
Thermal Denaturation ◽  
Force Microscopy ◽  
Atomic Force ◽  
Structure Changes ◽  
Intensity Changes ◽  
Amyloid Diseases

Transthyretin (TTR) aggregation has been characterized to be responsible for several amyloid diseases. Fourier transform infrared (FTIR) spectroscopy, fluorescence, and atomic force microscopy (AFM) are used to investigate secondary structure changes in transthyretin, induced upon thermal denaturation and interaction with pentobarbital. Spectral analysis revealed a strong static quenching of the intrinsic fluorescence of TTR by pentobarbital with a binding constant (K) estimated at2.092×103 M-1. Fourier self-deconvolution (FSD) technique is used to evaluates intensity changes in the spectra of the component bands in the amide I and amide II regions due to the changes in pentobarbital concentration in the protein complex. The increases of the relative intensities of the peaks at 1614 cm−1and 1507 cm−1are due to the increase of pentobarbital concentrations which is linked to the formation of oligomers in the protein.

scholarly journals Single-Molecule Reconstruction of Oligonucleotide Secondary Structure by Atomic Force Microscopy

Small ◽  
2014 ◽  
Vol 10 (16) ◽  
pp. 3257-3261 ◽  
Author(s):  
Alice Pyne ◽  
Ruth Thompson ◽  
Carl Leung ◽  
Debdulal Roy ◽  
Bart W. Hoogenboom
Keyword(s):  
Atomic Force Microscopy ◽  
Secondary Structure ◽  
Single Molecule ◽  
Force Microscopy ◽  
Atomic Force

Secondary Structure of α-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy

2006 ◽  
Vol 355 (1) ◽  
pp. 63-71 ◽  
Author(s):  
Mihaela M. Apetri ◽  
Nakul C. Maiti ◽  
Michael G. Zagorski ◽  
Paul R. Carey ◽  
Vernon E. Anderson
Keyword(s):  
Atomic Force Microscopy ◽  
Secondary Structure ◽  
Force Microscopy ◽  
Atomic Force

Atomic force microscopy analysis shows surface structure changes in carvacrol-treated bacterial cells

2011 ◽  
Vol 162 (2) ◽  
pp. 164-172 ◽  
Author(s):  
Antonietta La Storia ◽  
Danilo Ercolini ◽  
Francesco Marinello ◽  
Rosangela Di Pasqua ◽  
Francesco Villani ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Structure ◽  
Bacterial Cells ◽  
Atomic Force Microscopy Analysis ◽  
Force Microscopy ◽  
Atomic Force ◽  
Structure Changes ◽  
Microscopy Analysis

scholarly journals Chiral nanostructure in polymers under different deposition conditions observed using atomic force microscopy of monolayers: poly(phenylacetylene)s as a case study

2017 ◽  
Vol 53 (3) ◽  
pp. 481-492 ◽  
Author(s):  
F. Freire ◽  
E. Quiñoá ◽  
R. Riguera
Keyword(s):  
Atomic Force Microscopy ◽  
Secondary Structure ◽  
Force Microscopy ◽  
Atomic Force ◽  
Deposition Conditions

Techniques used for the study of the secondary structure of polymers by means of atomic-force microscopy are evaluated.

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