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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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 |
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English |
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Assfalg, Michael |
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Assfalg, Michael |
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title |
Protein Adsorption and Conformational Changes |
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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 |
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Protein Adsorption and Conformational Changes |
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Protein Adsorption and Conformational Changes |
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protein adsorption and conformational changes |
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MDPI - Multidisciplinary Digital Publishing Institute |
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2022 |
physical |
1 electronic resource (100 p.) |
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3-0365-2691-9 3-0365-2690-0 |
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Not Illustrated |
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AT assfalgmichael proteinadsorptionandconformationalchanges |
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(CKB)5680000000037719 (oapen)https://directory.doabooks.org/handle/20.500.12854/81201 (EXLCZ)995680000000037719 |
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Protein Adsorption and Conformational Changes |
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