Coping with low pH: molecular strategies in neutralophilic bacteria

P Lund, A Tramonti, D De Biase - FEMS microbiology reviews, 2014 - academic.oup.com
As part of their life cycle, neutralophilic bacteria are often exposed to varying environmental
stresses, among which fluctuations in pH are the most frequent. In particular, acid …

[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 …

Effect of pH-shifting treatment on structural and heat induced gel properties of peanut protein isolate

J Li, M Wu, Y Wang, K Li, J Du, Y Bai - Food Chemistry, 2020 - Elsevier
Modifying proteins with new methods to improve their functional properties is essential to
extend their application in food related field. In this study, the effect of pH-shifting treatment …

Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein: a possible molecular link between Parkinson′ s disease and heavy …

VN Uversky, J Li, AL Fink - Journal of Biological Chemistry, 2001 - ASBMB
Parkinson's disease involves the aggregation of α-synuclein to form fibrils, which are the
major constituent of intracellular protein inclusions (Lewy bodies and Lewy neurites) in …

Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions

NJ Greenfield - Nature protocols, 2006 - nature.com
Circular dichroism (CD) is an excellent spectroscopic technique for following the unfolding
and folding of proteins as a function of temperature. One of its principal applications is to …

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 …

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 …

Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes

J Jiang, J Chen, YL Xiong - Journal of agricultural and food …, 2009 - ACS Publications
Structural unfolding of soy protein isolate (SPI) as induced by holding (0, 0.5, 1, 2, and 4 h)
in acidic (pH 1.5− 3.5) and alkaline (pH 10.0− 12.0) pH solutions, followed by refolding (1 h) …

Stability matters, too–the thermodynamics of amyloid fibril formation

AK Buell - Chemical Science, 2022 - pubs.rsc.org
Amyloid fibrils are supramolecular homopolymers of proteins that play important roles in
biological functions and disease. These objects have received an exponential increase in …

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 …