Protein Adsorption and Conformational Changes

Protein adsorption to solids, nanomaterials, and biological surfaces is of central interest in many fields, including biomedicine, bioanalytical chemistry, materials engineering, bio-nanotechnology, and basic biomolecular research. Although protein adsorption may sometimes occur with little conseque...

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Year of Publication:2022
Language:English
Physical Description:1 electronic resource (100 p.)
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spelling Assfalg, Michael edt
Protein Adsorption and Conformational Changes
Basel MDPI - Multidisciplinary Digital Publishing Institute 2022
1 electronic resource (100 p.)
text txt rdacontent
computer c rdamedia
online resource cr rdacarrier
Protein adsorption to solids, nanomaterials, and biological surfaces is of central interest in many fields, including biomedicine, bioanalytical chemistry, materials engineering, bio-nanotechnology, and basic biomolecular research. Although protein adsorption may sometimes occur with little consequence on molecular structure, interactions with surfaces frequently cause changes in local or global conformations and dynamics, perturbations to secondary structures or tertiary folds, eventually resulting in dramatically altered protein function. Importantly, surfaces may trigger protein misfolding and self-aggregation, or, conversely, promote protein structure formation. The use of nanoscale surfaces to remodel the conformational landscape and the aggregation pathways of amyloidogenic peptides and proteins has been proposed as a promising strategy against several severe human diseases. The rapid growth of applications and technological innovation which is based on or concerned with protein adsorption necessitates renewed efforts to provide molecular-level insights into adsorption-induced protein structural perturbations. In this Special Issue, we gathered the recent findings of experimental and computational investigations that contributed novel insights into protein adsorption with a focus on the structural and dynamic aspects of proteins.
English
Research & information: general bicssc
Biology, life sciences bicssc
Biochemistry bicssc
sarcoplasmic reticulum Ca2+-ATPase
Cu+-ATPase
phospholipid flippase
charge displacement
concentration jump
solid supported membrane
conformational transition
electrogenicity
ion translocation
phospholipid flipping
protein-nanoparticle interactions
protein NMR
amyloidogenic proteins
nitroxide paramagnetic perturbation
spin label extrinsic probes
Tempol
β2-microglobulin
protein conformation
protein-surface association
lipid membranes
surface-immobilized protein
EPR spectroscopy
alpha-synuclein
amyloid fibrils
conformational flexibility
protein adsorption
protein aggregation
nano-bio interface
nanocomposite
nanoparticles
supramolecular assembly
NMR spectroscopy
gold nanoparticles
PEGylation
adsorption
passivation
3-0365-2691-9
3-0365-2690-0
Assfalg, Michael oth
language English
format eBook
author2 Assfalg, Michael
author_facet Assfalg, Michael
author2_variant m a ma
author2_role Sonstige
title Protein Adsorption and Conformational Changes
spellingShingle Protein Adsorption and Conformational Changes
title_full Protein Adsorption and Conformational Changes
title_fullStr Protein Adsorption and Conformational Changes
title_full_unstemmed Protein Adsorption and Conformational Changes
title_auth Protein Adsorption and Conformational Changes
title_new Protein Adsorption and Conformational Changes
title_sort protein adsorption and conformational changes
publisher MDPI - Multidisciplinary Digital Publishing Institute
publishDate 2022
physical 1 electronic resource (100 p.)
isbn 3-0365-2691-9
3-0365-2690-0
illustrated Not Illustrated
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is_hierarchy_title Protein Adsorption and Conformational Changes
author2_original_writing_str_mv noLinkedField
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