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dc.contributor.editorAssfalg, Michael
dc.date.accessioned2022-05-06T11:35:02Z
dc.date.available2022-05-06T11:35:02Z
dc.date.issued2022
dc.identifierONIX_20220506_9783036526911_267
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/81201
dc.description.abstractProtein 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.
dc.languageEnglish
dc.subject.classificationbic Book Industry Communication::G Reference, information & interdisciplinary subjects::GP Research & information: general
dc.subject.classificationbic Book Industry Communication::P Mathematics & science::PS Biology, life sciences
dc.subject.classificationbic Book Industry Communication::P Mathematics & science::PS Biology, life sciences::PSB Biochemistry
dc.subject.othersarcoplasmic reticulum Ca2+-ATPase
dc.subject.otherCu+-ATPase
dc.subject.otherphospholipid flippase
dc.subject.othercharge displacement
dc.subject.otherconcentration jump
dc.subject.othersolid supported membrane
dc.subject.otherconformational transition
dc.subject.otherelectrogenicity
dc.subject.otherion translocation
dc.subject.otherphospholipid flipping
dc.subject.otherprotein-nanoparticle interactions
dc.subject.otherprotein NMR
dc.subject.otheramyloidogenic proteins
dc.subject.othernitroxide paramagnetic perturbation
dc.subject.otherspin label extrinsic probes
dc.subject.otherTempol
dc.subject.otherβ2-microglobulin
dc.subject.otherprotein conformation
dc.subject.otherprotein-surface association
dc.subject.otherlipid membranes
dc.subject.othersurface-immobilized protein
dc.subject.otherEPR spectroscopy
dc.subject.otheralpha-synuclein
dc.subject.otheramyloid fibrils
dc.subject.otherconformational flexibility
dc.subject.otherprotein adsorption
dc.subject.otherprotein aggregation
dc.subject.othernano-bio interface
dc.subject.othernanocomposite
dc.subject.othernanoparticles
dc.subject.othersupramolecular assembly
dc.subject.otherNMR spectroscopy
dc.subject.othergold nanoparticles
dc.subject.otherPEGylation
dc.subject.otheradsorption
dc.subject.otherpassivation
dc.subject.othern/a
dc.titleProtein Adsorption and Conformational Changes
dc.typebook
oapen.identifier.doi10.3390/books978-3-0365-2690-4
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn9783036526911
oapen.relation.isbn9783036526904
oapen.pages100
oapen.place.publicationBasel


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