The application of circular dichroism to studies of protein folding and unfolding

SM Kelly, NC Price - Biochimica et Biophysica Acta (BBA)-Protein Structure …, 1997 - Elsevier
In this review, we shall outline the basic principles Ž. of circular dichroism CD and indicate
the types of structural information relevant to the study of the Ž. folding and unfolding or …

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 …

Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to …

P Luo, RL Baldwin - Biochemistry, 1997 - ACS Publications
To establish a framework for extrapolating the helix-forming properties of peptides from
TFE/H2O mixtures (TFE= 2, 2, 2-trifluoroethanol) back to water, the thermal unfolding curves …

Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein

J Li, VN Uversky, AL Fink - Biochemistry, 2001 - ACS Publications
Parkinson's disease involves the loss of dopaminergic neurons in the substantia nigra,
leading to movement disorders. The pathological hallmark of Parkinson's disease is the …

[图书][B] The structure of biological membranes

PL Yeagle - 2004 - taylorfrancis.com
Recent research has provided an abundance of new information on membrane
biochemistry. Now more than ever, it is essential to update our current understanding of …

Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides

DP Hong, M Hoshino, R Kuboi… - Journal of the American …, 1999 - ACS Publications
Among various alcohols, those substituted with fluorine, such as 2, 2, 2-trifluoroethanol
(TFE) or 3, 3, 3, 3 ', 3 ', 3 '-hexafluoro-2-propanol (HFIP), have a marked potential to induce …

Role of the molten globule state in protein folding

M Arai, K Kuwajima - Advances in protein chemistry, 2000 - Elsevier
Publisher Summary This chapter deals with the structure of the molten globules of various
globular proteins revealed by the recent experimental studies. Recent advances in …

Protein folding in the landscape perspective: Chevron plots and non‐Arrhenius kinetics

HS Chan, KA Dill - Proteins: Structure, Function, and …, 1998 - Wiley Online Library
We use two simple models and the energy landscape perspective to study protein folding
kinetics. A major challenge has been to use the landscape perspective to interpret …

Conformational behavior and aggregation of α-synuclein in organic solvents: modeling the effects of membranes

LA Munishkina, C Phelan, VN Uversky, AL Fink - Biochemistry, 2003 - ACS Publications
Intracellular proteinaceous inclusions (Lewy bodies and Lewy neurites) of α-synuclein are
pathological hallmarks of neurodegenerative diseases such as Parkinson's disease …

Cooperative α‐helix formation of β‐lactoglobulin and melittin induced by hexafluoroisopropanol

N Hirota, Y Goto, K Mizuno - Protein science, 1997 - Wiley Online Library
Alcohols denature the native state of proteins, and also stabilize the α‐helical conformation
in unfolded proteins and peptides. Among various alcohols, trifluoroethanol (TFE) and …