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 Changes3037214UNINA01887nam2 22003733i 450 VAN024244320240423091549.97N978366247940720220308d2015 |0itac50 baengCH|||| |||||ˆ1: ‰Biosynthesis, structural diversity and sialoglycopathologiesRita Gerardy-Schahn, Philippe Delannoy, Mark von ItzsteinChamSpringer2015IX, 211 p.ill.24 cm001VAN00712532001 Topics in current chemistry210 BerlinSpringer366001VAN02424422001 SialoGlyco Chemistry and BiologyRita Gerardy-Schahn, Philippe Delannoy, Mark von Itzstein210 ChamSpringer2015215 volumiill.24 cm1CHChamVANL001889572Biochimica. Citochimica. Istochimica22540Chimica generale22571.6Biologia cellulare22661Chimica organica applicata22Gerardy-SchahnRitaVANV198296933788DelannoyPhilippeVANV1982971207414Von ItzsteinMarkVANV1982981207415Springer <editore>VANV108073650ITSOL20240614RICAhttps://rd.springer.com/book/10.1007/978-3-662-47940-7E-book - Accesso al full-text attraverso riconoscimento IP di Ateneo, proxy e/o ShibbolethBIBLIOTECA DEL DIPARTIMENTO DI SCIENZE E TECNOLOGIE AMBIENTALI BIOLOGICHE E FARMACEUTICHEIT-CE0101VAN17NVAN0242443BIBLIOTECA DEL DIPARTIMENTO DI SCIENZE E TECNOLOGIE AMBIENTALI BIOLOGICHE E FARMACEUTICHE17CONS e-book 2219 17BIB2219/148 148 20220308 Biosynthesis, structural diversity and sialoglycopathologies2785126UNICAMPANIA