Role of lipids in the interaction of antimicrobial peptides with membranes

V Teixeira, MJ Feio, M Bastos - Progress in lipid research, 2012 - Elsevier
Antimicrobial peptides (AMPs) take part in the immune system by mounting a first line of
defense against pathogens. Recurrent structural and functional aspects are observed …

Principles of protein folding—a perspective from simple exact models

KA Dill, S Bromberg, K Yue, HS Chan… - Protein …, 1995 - Wiley Online Library
General principles of protein structure, stability, and folding kinetics have recently been
explored in computer simulations of simple exact lattice models. These models represent …

Optimized molecular dynamics force fields applied to the helix− coil transition of polypeptides

RB Best, G Hummer - The journal of physical chemistry B, 2009 - ACS Publications
Obtaining the correct balance of secondary structure propensities is a central priority in
protein force-field development. Given that current force fields differ significantly in their α …

Coupling of local folding to site-specific binding of proteins to DNA

RS Spolar, MT Record Jr - Science, 1994 - science.org
Thermodynamic studies have demonstrated the central importance of a large negative heat
capacity change (Δ C° assoc) in site-specific protein-DNA recognition. Dissection of the …

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 …

Elucidating the folding problem of helical peptides using empirical parameters

V Muñoz, L Serrano - Nature structural biology, 1994 - nature.com
Using an empirical analysis of experimental data we have estimated a set of energy
contributions which accounts for the stability of isolated α-helices. With this database and an …

Solvophobically driven folding of nonbiological oligomers

JC Nelson, JG Saven, JS Moore, PG Wolynes - Science, 1997 - science.org
In solution, biopolymers commonly fold into well-defined three-dimensional structures, but
only recently has analogous behavior been explored in synthetic chain molecules. An …

Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactions

A Chakrabartty, T Kortemme, RL Baldwin - Protein Science, 1994 - Wiley Online Library
Helix propensities of the amino acids have been measured in alanine‐based peptides in the
absence of helix‐stabilizing side‐chain interactions. Fifty‐eight peptides have been studied …

The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding

T Bartels, LS Ahlstrom, A Leftin, F Kamp, C Haass… - Biophysical journal, 2010 - cell.com
Alpha-synuclein (αS) is a 140-amino-acid protein that is involved in a number of
neurodegenerative diseases. In Parkinson's disease, the protein is typically encountered in …

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 …