03852nam 2200805z- 450 991056646610332120231214133325.0(CKB)5680000000037719(oapen)https://directory.doabooks.org/handle/20.500.12854/81201(EXLCZ)99568000000003771920202205d2022 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierProtein Adsorption and Conformational ChangesBaselMDPI - Multidisciplinary Digital Publishing Institute20221 electronic resource (100 p.)3-0365-2691-9 3-0365-2690-0 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.Research & information: generalbicsscBiology, life sciencesbicsscBiochemistrybicsscsarcoplasmic reticulum Ca2+-ATPaseCu+-ATPasephospholipid flippasecharge displacementconcentration jumpsolid supported membraneconformational transitionelectrogenicityion translocationphospholipid flippingprotein-nanoparticle interactionsprotein NMRamyloidogenic proteinsnitroxide paramagnetic perturbationspin label extrinsic probesTempolβ2-microglobulinprotein conformationprotein-surface associationlipid membranessurface-immobilized proteinEPR spectroscopyalpha-synucleinamyloid fibrilsconformational flexibilityprotein adsorptionprotein aggregationnano-bio interfacenanocompositenanoparticlessupramolecular assemblyNMR spectroscopygold nanoparticlesPEGylationadsorptionpassivationResearch & information: generalBiology, life sciencesBiochemistryAssfalg Michaeledt1326249Assfalg MichaelothBOOK9910566466103321Protein Adsorption and Conformational Changes3037214UNINA