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High-resolution 2D 1H- 15N NMR characterization of persistent structural alterations of proteins induced by interactions with silica nanoparticles

Lundqvist, Martin LU ; Sethson, Ingmar and Jonsson, Bengt-Harald (2005) In Langmuir 21(13). p.5974-5979
Abstract
The binding of protein to solid surfaces often induces changes in the structure, and to investigate these matters we have selected two different protein−nanoparticle systems. The first system concerns the enzyme human carbonic anhydrase II which binds essentially irreversibly to the nanoparticles, and the second system concerns human carbonic anhydrase I which alternate between the adsorbed and free state upon interaction with nanoparticles. Application of the TROSY pulse sequence has allowed high-resolution NMR analysis for both of the protein−nanoparticle systems. For HCAII it was possible to observe spectra of protein when bound to the nanoparticles. The results indicated that HCAII undergoes large rearrangements, forming an ensemble of... (More)
The binding of protein to solid surfaces often induces changes in the structure, and to investigate these matters we have selected two different protein−nanoparticle systems. The first system concerns the enzyme human carbonic anhydrase II which binds essentially irreversibly to the nanoparticles, and the second system concerns human carbonic anhydrase I which alternate between the adsorbed and free state upon interaction with nanoparticles. Application of the TROSY pulse sequence has allowed high-resolution NMR analysis for both of the protein−nanoparticle systems. For HCAII it was possible to observe spectra of protein when bound to the nanoparticles. The results indicated that HCAII undergoes large rearrangements, forming an ensemble of molten globule-like structures on the surface. The spectra from the HCAI−nanoparticle system are dominated by HCAI molecules in solution. A comparative analysis of variations in intensity from 97 amide resonances in a 1H−15N TROSY spectrum revealed the effects from interaction with nanoparticle on the protein structure at amino acid resolution. (Less)
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author
; and
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
21
issue
13
pages
6 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:21644473108
ISSN
0743-7463
DOI
10.1021/la050569j
language
English
LU publication?
no
id
2068fa4e-4c3d-48e4-ab08-4c91c4ff08d1
date added to LUP
2021-10-19 11:41:17
date last changed
2022-02-02 00:39:26
@article{2068fa4e-4c3d-48e4-ab08-4c91c4ff08d1,
  abstract     = {{The binding of protein to solid surfaces often induces changes in the structure, and to investigate these matters we have selected two different protein−nanoparticle systems. The first system concerns the enzyme human carbonic anhydrase II which binds essentially irreversibly to the nanoparticles, and the second system concerns human carbonic anhydrase I which alternate between the adsorbed and free state upon interaction with nanoparticles. Application of the TROSY pulse sequence has allowed high-resolution NMR analysis for both of the protein−nanoparticle systems. For HCAII it was possible to observe spectra of protein when bound to the nanoparticles. The results indicated that HCAII undergoes large rearrangements, forming an ensemble of molten globule-like structures on the surface. The spectra from the HCAI−nanoparticle system are dominated by HCAI molecules in solution. A comparative analysis of variations in intensity from 97 amide resonances in a <sup>1</sup>H−<sup>15</sup>N TROSY spectrum revealed the effects from interaction with nanoparticle on the protein structure at amino acid resolution.}},
  author       = {{Lundqvist, Martin and Sethson, Ingmar and Jonsson, Bengt-Harald}},
  issn         = {{0743-7463}},
  language     = {{eng}},
  number       = {{13}},
  pages        = {{5974--5979}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Langmuir}},
  title        = {{High-resolution 2D <sup>1</sup>H- <sup>15</sup>N NMR characterization of persistent structural alterations of proteins induced by interactions with silica nanoparticles}},
  url          = {{http://dx.doi.org/10.1021/la050569j}},
  doi          = {{10.1021/la050569j}},
  volume       = {{21}},
  year         = {{2005}},
}