Results 41 to 50 of about 1,516,213 (305)
Dependence of Self-Assembled Peptide Hydrogel Network Structure on Local Fibril Nanostructure [PDF]
Physically cross-linked, fibrillar hydrogel networks are formed by the self-assembly of β-hairpin peptide molecules with varying degrees of strand asymmetry.
Hammouda, Boualem +4 more
core +2 more sources
Antibacterial peptides (APMs) are a new type of antibacterial substance. The relationship between their structure and function remains indistinct; in particular, there is a lack of a definitive and fixed template for designing new antimicrobial peptides.
N. Dong +7 more
semanticscholar +1 more source
CRANKITE: a fast polypeptide backbone conformation sampler [PDF]
Background: CRANKITE is a suite of programs for simulating backbone conformations of polypeptides and proteins. The core of the suite is an efficient Metropolis Monte Carlo sampler of backbone conformations in continuous three-dimensional space in atomic
A Elofsson +19 more
core +4 more sources
The two-domain protein RfaH, a paralog of the universally conserved NusG/Spt5 transcription factors, is regulated by autoinhibition coupled to the reversible conformational switch of its 60-residue C-terminal Kyrpides, Ouzounis, Woese (KOW) domain ...
Philipp K Zuber +5 more
doaj +1 more source
Solution and Micelle-Bound Structures of Tachyplesin I and Its Active Aromatic Linear Derivatives [PDF]
Tachyplesin I is a 17-residue peptide isolated from the horseshoe crab, Tachyplesus tridentatus. It has high antimicrobial activity and adopts a β-hairpin conformation in solution stabilized by two cross-strand disulfide bonds.
Andreotti, Amy +3 more
core +3 more sources
Bacteria have acquired extensive resistance mechanisms to protect themselves against antibiotic action. Today the bacterial membrane has become one of the “final frontiers” in the search for new compounds acting on novel targets to address the threat of ...
I. Edwards +5 more
semanticscholar +1 more source
Structure of the NheA component of the Nhe toxin from Bacillus cereus: implications for function.
The structure of NheA, a component of the Bacillus cereus Nhe tripartite toxin, has been solved at 2.05 Å resolution using selenomethionine multiple-wavelength anomalous dispersion (MAD).
Magdah Ganash +5 more
doaj +1 more source
The insertion of azobenzene moiety in complex molecular protein or peptide systems can lead to molecular switches to be used to determine kinetics of folding/unfolding properties of secondary structures, such as α-helix, β-turn, or β-hairpin. In fact, in
Francesca Nuti +14 more
doaj +1 more source
Five series (28 structures) of photoswitchable β-hairpin peptides were synthesized based on the cyclic scaffold of the natural antibiotic gramicidin S. Cell-type selectivity was compared for all activated (diarylethene "ring-open") and deactivated ("ring-
O. Babii +9 more
semanticscholar +1 more source
An exactly solvable model for a beta-hairpin with random interactions
I investigate a disordered version of a simplified model of protein folding, with binary degrees of freedom, applied to an ideal beta-hairpin structure.
Edwards S F +6 more
core +1 more source

