Mass spectrometry using electrospray ionization

GRD Prabhu, ER Williams, M Wilm… - Nature Reviews Methods …, 2023 - nature.com
Applying a high voltage to a liquid passing through a capillary disintegrates the liquid
meniscus to generate a fine spray of charged droplets. As the droplets evaporate, polar …

[HTML][HTML] α-Synuclein misfolding and Parkinson's disease

L Breydo, JW Wu, VN Uversky - … et Biophysica Acta (BBA)-Molecular Basis …, 2012 - Elsevier
Substantial evidence links α-synuclein, a small highly conserved presynaptic protein with
unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has …

Multifunctional Cytochrome c: Learning New Tricks from an Old Dog

D Alvarez-Paggi, L Hannibal, MA Castro… - Chemical …, 2017 - ACS Publications
Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible
structure, particularly in the ferric form, such that it is able to sample a broad conformational …

Why are “natively unfolded” proteins unstructured under physiologic conditions?

VN Uversky, JR Gillespie… - Proteins: structure, function …, 2000 - Wiley Online Library
Abstract “Natively unfolded” proteins occupy a unique niche within the protein kingdom in
that they lack ordered structure under conditions of neutral pH in vitro. Analysis of amino …

Globular proteins as soft particles for stabilizing emulsions: Concepts and strategies

CH Tang - Food Hydrocolloids, 2020 - Elsevier
Many globular proteins are good emulsifiers or stabilizers for oil-in-water emulsions. It is
generally recognized in the field that globular proteins tend to undergo a structural unfolding …

Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism

L Nielsen, R Khurana, A Coats, S Frokjaer… - Biochemistry, 2001 - ACS Publications
In the search for the molecular mechanism of insulin fibrillation, the kinetics of insulin fibril
formation were studied under different conditions using the fluorescent dye thioflavin T …

Intrinsically disordered proteins from A to Z

VN Uversky - The international journal of biochemistry & cell biology, 2011 - Elsevier
The ideas that proteins might possess specific functions without being uniquely folded into
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …

What does it mean to be natively unfolded?

VN Uversky - European journal of biochemistry, 2002 - Wiley Online Library
Natively unfolded or intrinsically unstructured proteins constitute a unique group of the
protein kingdom. The evolutionary persistence of such proteins represents strong evidence …

Molten globule and protein folding

OB Ptitsyn - Advances in protein chemistry, 1995 - Elsevier
Publisher Summary This chapter describes the present state of the studies of the molten
globule state and its role in protein folding and physiological processes. Recent data on the …

The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid

Z Lai, W Colón, JW Kelly - Biochemistry, 1996 - ACS Publications
Transthyretin (TTR) amyloid fibril formation is observed during partial acid denaturation and
while refolding acid-denatured TTR, implying that amyloid fibril formation results from the …