From Levinthal to pathways to funnels

KA Dill, HS Chan - Nature structural biology, 1997 - nature.com
From Levinthalto pathways to funnels Page 1 TS 9 1997 Nature Publishing Group http://www.nature.com/nsmb
perspective From Levinthalto pathways to funnels Ken A. Dill and Hue Sun Chan A new …

Polymer principles and protein folding

KA Dill - Protein Science, 1999 - cambridge.org
This paper surveys the emerging role of statistical mechanics and polymer theory in protein
folding. In the polymer perspective, the folding code is more a solvation code than a code of …

[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 …

The core lipocalin, bovine β-lactoglobulin

L Sawyer, G Kontopidis - Biochimica et Biophysica Acta (BBA)-Protein …, 2000 - Elsevier
The lipocalin family became established shortly after the structural similarity was noted
between plasma retinol binding protein and the bovine milk protein, β-lactoglobulin. During …

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 …

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 …

Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins

N Hirota, K Mizuno, Y Goto - Journal of molecular biology, 1998 - Elsevier
Detailed analysis of the effects of alcohols on proteins and peptides is important because of
its wide range of applications in many fields. Whereas melittin, a major component of …

Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein

D Hamada, S Segawa, Y Goto - nature structural biology, 1996 - nature.com
It is generally assumed that folding intermediates contain partially formed native-like
secondary structures. However, if we consider the fact that the conformational stability of the …

Coupled prediction of protein secondary and tertiary structure

J Meiler, D Baker - Proceedings of the National Academy of …, 2003 - National Acad Sciences
The strong coupling between secondary and tertiary structure formation in protein folding is
neglected in most structure prediction methods. In this work we investigate the extent to …

Salt‐dependent monomer–dimer equilibrium of bovine β‐lactoglobulin at pH 3

K Sakurai, M Oobatake, Y Goto - Protein Science, 2001 - Wiley Online Library
Although bovine β‐lactoglobulin assumes a monomeric native structure at pH 3 in the
absence of salt, the addition of salts stabilizes the dimer. Thermodynamics of the monomer …