LEADER 03889nam 2200829z- 450 001 9910566466103321 005 20220506 035 $a(CKB)5680000000037719 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/81201 035 $a(oapen)doab81201 035 $a(EXLCZ)995680000000037719 100 $a20202205d2022 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$aProtein Adsorption and Conformational Changes 210 $aBasel$cMDPI - Multidisciplinary Digital Publishing Institute$d2022 215 $a1 online resource (100 p.) 311 08$a3-0365-2691-9 311 08$a3-0365-2690-0 330 $aProtein 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. 606 $aBiochemistry$2bicssc 606 $aBiology, life sciences$2bicssc 606 $aResearch & information: general$2bicssc 610 $aadsorption 610 $aalpha-synuclein 610 $aamyloid fibrils 610 $aamyloidogenic proteins 610 $acharge displacement 610 $aconcentration jump 610 $aconformational flexibility 610 $aconformational transition 610 $aCu+-ATPase 610 $aelectrogenicity 610 $aEPR spectroscopy 610 $agold nanoparticles 610 $aion translocation 610 $alipid membranes 610 $an/a 610 $anano-bio interface 610 $ananocomposite 610 $ananoparticles 610 $anitroxide paramagnetic perturbation 610 $aNMR spectroscopy 610 $apassivation 610 $aPEGylation 610 $aphospholipid flippase 610 $aphospholipid flipping 610 $aprotein adsorption 610 $aprotein aggregation 610 $aprotein conformation 610 $aprotein NMR 610 $aprotein-nanoparticle interactions 610 $aprotein-surface association 610 $asarcoplasmic reticulum Ca2+-ATPase 610 $asolid supported membrane 610 $aspin label extrinsic probes 610 $asupramolecular assembly 610 $asurface-immobilized protein 610 $aTempol 610 $a?2-microglobulin 615 7$aBiochemistry 615 7$aBiology, life sciences 615 7$aResearch & information: general 700 $aAssfalg$b Michael$4edt$01326249 702 $aAssfalg$b Michael$4oth 906 $aBOOK 912 $a9910566466103321 996 $aProtein Adsorption and Conformational Changes$93037214 997 $aUNINA