[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 …

Understanding protein non-folding

VN Uversky, AK Dunker - Biochimica et Biophysica Acta (BBA)-Proteins …, 2010‏ - Elsevier
This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …

Natively unfolded proteins: a point where biology waits for physics

VN Uversky - Protein science, 2002‏ - Wiley Online Library
The experimental material accumulated in the literature on the conformational behavior of
intrinsically unstructured (natively unfolded) proteins was analyzed. Results of this analysis …

Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques

DK Wilkins, SB Grimshaw, V Receveur, CM Dobson… - Biochemistry, 1999‏ - ACS Publications
Pulse field gradient NMR methods have been used to determine the effective hydrodynamic
radii of a range of native and nonnative protein conformations. From these experimental …

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 …

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein− ligand binding

VM Krishnamurthy, GK Kaufman, AR Urbach… - Chemical …, 2008‏ - ACS Publications
Carbonic anhydrase (CA, EC 4.2. 1.1) is a protein that is especially well-suited to serve as a
model in many types of studies in biophysics, bioanalysis, the physical-organic chemistry of …

[HTML][HTML] α-Lactalbumin: structure and function

EA Permyakov, LJ Berliner - FEBS letters, 2000‏ - Elsevier
Small milk protein α-lactalbumin (α-LA), a component of lactose synthase, is a simple model
Ca2+ binding protein, which does not belong to the EF-hand proteins, and a classical …

Design and Synthesis of a Water‐Stable Anionic Uranium‐Based Metal–Organic Framework (MOF) with Ultra Large Pores

P Li, NA Vermeulen, X Gong, CD Malliakas… - Angewandte …, 2016‏ - Wiley Online Library
Ionic metal–organic frameworks (MOFs) are a subclass of porous materials that have the
ability to incorporate different charged species in confined nanospace by ion‐exchange. To …

[PDF][PDF] Probing protein structure by limited proteolysis

A Fontana… - Acta Biochimica …, 2004‏ - frontierspartnerships.org
Limited proteolysis experiments can be successfully used to probe conformational features
of proteins. In a number of studies it has been demonstrated that the sites of limited …

Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and …

VN Uversky - The protein journal, 2009‏ - Springer
Intrinsically disordered proteins (IDPs) differ from “normal” ordered proteins at several levels,
structural, functional and conformational. Amino acid biases characteristic for IDPs …