Chirality is ubiquitous in nature with primary cellular functions that include construction of
right‐/left‐handed helix and selective communications among diverse biomolecules. Of …

Vibrational sum frequency spectroscopy (VSFS) was used to explore specific ion effects on
interfacial water structure adjacent to a bovine serum albumin (BSA) monolayer adsorbed at …

Cationic antimicrobial peptides (CAMPs) are important elements of innate immunity in
higher organisms, representing an ancient defense mechanism against pathogenic bacteria …

Among homopolypeptides, polyproline is unique due to its conformational flexibility between
right-handed PPI and left-handed PPII helices. Herein, we designed a propargyloxy …

The expansion of homopolymeric glutamine (polyQ) or alanine (polyA) repeats in certain
proteins owing to genetic mutations induces protein aggregation and toxicity, causing at …

Inter-amino acid residues electrostatic interactions contribute to the conformational stability
of peptides and proteins, influence their folding pathways, and are critically important to a …

Polyalanine (polyA) is the third-most prevalent homopeptide repeat in eukaryotes, behind
polyglutamine and polyasparagine. Abnormal expansion of the polyA repeat is linked to at …

Circular dichroism (CD) and attenuated total reflectance Fourier-transform infrared (ATR-
FTIR) spectroscopies were used to study how sucrose and salts, NaCl, NaClO 4, Na 2 SO 4 …

We investigate the role of dynamics on adsorption of peptides to gold surfaces using all-
atom molecular dynamics simulations in explicit solvent. We choose six homopolypeptides …

Proteins interact with ions in various ways. The surface of proteins has an innate capability
to bind ions, and it is also influenced by the screening of the electrostatic potential owing to …