Explore
Protein Adsorption and Conformational Changes
0 Ungluers have
Faved this Work
Login to Fave
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.
This book is included in DOAB.
Why read this book? Have your say.
You must be logged in to comment.
Rights Information
Are you the author or publisher of this work? If so, you can claim it as yours by registering as an Unglue.it rights holder.Downloads
This work has been downloaded 24 times via unglue.it ebook links.
- 24 - pdf (CC BY) at Unglue.it.
Keywords
- adsorption
- alpha-Synuclein
- amyloid fibrils
- amyloidogenic proteins
- Biochemistry
- Biology, Life Sciences
- charge displacement
- concentration jump
- conformational flexibility
- conformational transition
- Cu+-ATPase
- electrogenicity
- EPR spectroscopy
- gold nanoparticles
- ion translocation
- lipid membranes
- Mathematics & science
- n/a
- nano-bio interface
- nanocomposite
- Nanoparticles
- nitroxide paramagnetic perturbation
- NMR spectroscopy
- passivation
- pegylation
- phospholipid flippase
- phospholipid flipping
- protein adsorption
- protein aggregation
- Protein Conformation
- protein NMR
- protein-nanoparticle interactions
- protein-surface association
- Reference, information & interdisciplinary subjects
- Research & information: general
- sarcoplasmic reticulum Ca2+-ATPase
- solid supported membrane
- spin label extrinsic probes
- supramolecular assembly
- surface-immobilized protein
- Tempol
- β2-microglobulin
Links
DOI: 10.3390/books978-3-0365-2690-4Editions