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 …

Gliadins from wheat grain: An overview, from primary structure to nanostructures of aggregates

R Urade, N Sato, M Sugiyama - Biophysical reviews, 2018 - Springer
Gliadins are well-known wheat grain proteins, particularly important in food science. They
were studied as early as the 1700s. Despite their long history, it has been difficult to identify …

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 …

Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro

R Kayed, J Bernhagen, N Greenfield… - Journal of molecular …, 1999 - Elsevier
Amyloid aggregates have been recognized to be a pathological hallmark of several fatal
diseases, including Alzheimer's disease, the prion-related diseases, and type II diabetes …

Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin

AS Ladokhin, SH White - Journal of molecular biology, 1999 - Elsevier
Membranes have a potent ability to promote secondary structure formation in a wide range
of membrane-active peptides, believed to be due to a reduction through hydrogen bonding …

Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange

M Hoshino, H Katou, Y Hagihara, K Hasegawa… - Nature structural …, 2002 - nature.com
Despite numerous efforts, the lack of detailed structural information on amyloid fibrils has
hindered clarification of the mechanism of their formation. Here, we describe a novel …

Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity

M Fernández-Vidal, S Jayasinghe, AS Ladokhin… - Journal of molecular …, 2007 - Elsevier
High amphiphilicity is a hallmark of interfacial helices in membrane proteins and membrane-
active peptides, such as toxins and antimicrobial peptides. Although there is general …

Komodo dragon-inspired synthetic peptide DRGN-1 promotes wound-healing of a mixed-biofilm infected wound

EMC Chung, SN Dean, CN Propst, BM Bishop… - npj Biofilms and …, 2017 - nature.com
Cationic antimicrobial peptides are multifunctional molecules that have a high potential as
therapeutic agents. We have identified a histone H1-derived peptide from the Komodo …

Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin S4 derivatives* 210

I Kustanovich, DE Shalev, M Mikhlin, L Gaidukov… - Journal of Biological …, 2002 - ASBMB
To better understand the structural requirements for selective cytotoxicity of antimicrobial
peptides, seven dermaseptin S4 analogs were produced and investigated with respect to …

Chemical interactions of polyethylene glycols (PEGs) and glycerol with protein functional groups: applications to effects of PEG and glycerol on protein processes

DB Knowles, IA Shkel, NM Phan, M Sternke… - Biochemistry, 2015 - ACS Publications
In this work, we obtain the data needed to predict chemical interactions of polyethylene
glycols (PEGs) and glycerol with proteins and related organic compounds and thereby …