Non-covalent Immobilization of Desmoplakin Plakin Domain Molecules by Size-Selected Clusters for AFM Imaging

P. Rodríguez-Zamora; J. Barreto; F. Yin; R. E. Palmer

doi:10.1007/s12668-014-0126-9

Non-covalent Immobilization of Desmoplakin Plakin Domain Molecules by Size-Selected Clusters for AFM Imaging

P. Rodríguez-Zamora^*, J. Barreto, F. Yin, R. E. Palmer

^*Corresponding author for this work

Research output: Contribution to journal › Article (Academic Journal) › peer-review

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Abstract

We exploit the immobilization of proteins by size-selected atomic gold clusters to examine the plakin domain of desmoplakin (PD), a human desmosomal protein that is mutated in severe skin diseases and cardiomyopathy, using atomic force microscopy (AFM) in the liquid phase. Contact mode AFM indicates that the PD does not establish a covalent bond size-selected gold nanocluster supported on a graphite substrate, but tapping mode AFM images indicate enhanced weak adsorption. The protein dimensions obtained are compared with predicted values based on electron microscopy, small-angle X-ray scattering (SAXS) and X-ray crystallographic studies.

Original language	English
Pages (from-to)	97-103
Number of pages	7
Journal	BioNanoScience
Volume	4
Issue number	2
DOIs	https://doi.org/10.1007/s12668-014-0126-9
Publication status	Published - 2014

Research Groups and Themes

Photonics and Quantum

Keywords

Atomic force microscopy
Desmoplakin plakin domain
Protein immobilization
Size-selected clusters

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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title = "Non-covalent Immobilization of Desmoplakin Plakin Domain Molecules by Size-Selected Clusters for AFM Imaging",

abstract = "We exploit the immobilization of proteins by size-selected atomic gold clusters to examine the plakin domain of desmoplakin (PD), a human desmosomal protein that is mutated in severe skin diseases and cardiomyopathy, using atomic force microscopy (AFM) in the liquid phase. Contact mode AFM indicates that the PD does not establish a covalent bond size-selected gold nanocluster supported on a graphite substrate, but tapping mode AFM images indicate enhanced weak adsorption. The protein dimensions obtained are compared with predicted values based on electron microscopy, small-angle X-ray scattering (SAXS) and X-ray crystallographic studies.",

keywords = "Atomic force microscopy, Desmoplakin plakin domain, Protein immobilization, Size-selected clusters",

author = "P. Rodr{\'i}guez-Zamora and J. Barreto and F. Yin and Palmer, {R. E.}",

year = "2014",

doi = "10.1007/s12668-014-0126-9",

language = "English",

volume = "4",

pages = "97--103",

journal = "BioNanoScience",

issn = "2191-1630",

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TY - JOUR

T1 - Non-covalent Immobilization of Desmoplakin Plakin Domain Molecules by Size-Selected Clusters for AFM Imaging

AU - Rodríguez-Zamora, P.

AU - Barreto, J.

AU - Yin, F.

AU - Palmer, R. E.

PY - 2014

Y1 - 2014

N2 - We exploit the immobilization of proteins by size-selected atomic gold clusters to examine the plakin domain of desmoplakin (PD), a human desmosomal protein that is mutated in severe skin diseases and cardiomyopathy, using atomic force microscopy (AFM) in the liquid phase. Contact mode AFM indicates that the PD does not establish a covalent bond size-selected gold nanocluster supported on a graphite substrate, but tapping mode AFM images indicate enhanced weak adsorption. The protein dimensions obtained are compared with predicted values based on electron microscopy, small-angle X-ray scattering (SAXS) and X-ray crystallographic studies.

AB - We exploit the immobilization of proteins by size-selected atomic gold clusters to examine the plakin domain of desmoplakin (PD), a human desmosomal protein that is mutated in severe skin diseases and cardiomyopathy, using atomic force microscopy (AFM) in the liquid phase. Contact mode AFM indicates that the PD does not establish a covalent bond size-selected gold nanocluster supported on a graphite substrate, but tapping mode AFM images indicate enhanced weak adsorption. The protein dimensions obtained are compared with predicted values based on electron microscopy, small-angle X-ray scattering (SAXS) and X-ray crystallographic studies.

KW - Atomic force microscopy

KW - Desmoplakin plakin domain

KW - Protein immobilization

KW - Size-selected clusters

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U2 - 10.1007/s12668-014-0126-9

DO - 10.1007/s12668-014-0126-9

M3 - Article (Academic Journal)

AN - SCOPUS:84899668028

SN - 2191-1630

VL - 4

SP - 97

EP - 103

JO - BioNanoScience

JF - BioNanoScience

IS - 2

ER -

Non-covalent Immobilization of Desmoplakin Plakin Domain Molecules by Size-Selected Clusters for AFM Imaging

Abstract

Research Groups and Themes

Keywords

UN SDGs

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