Results 41 to 50 of about 1,516,213 (305)

Dependence of Self-Assembled Peptide Hydrogel Network Structure on Local Fibril Nanostructure [PDF]

open access: yes, 2009
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

Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria

open access: yesInternational Journal of Molecular Sciences, 2019
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]

open access: yes, 2008
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

Structural and thermodynamic analyses of the β-to-α transformation in RfaH reveal principles of fold-switching proteins

open access: yeseLife, 2022
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]

open access: yes, 2002
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

Contribution of Amphipathicity and Hydrophobicity to the Antimicrobial Activity and Cytotoxicity of β-Hairpin Peptides

open access: yesACS Infectious Diseases, 2016
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.

open access: yesPLoS ONE, 2013
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

A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch

open access: yesFrontiers in Chemistry, 2019
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

Structure-Activity Relationships of Photoswitchable Diarylethene-Based β-Hairpin Peptides as Membranolytic Antimicrobial and Anticancer Agents.

open access: yesJournal of Medicinal Chemistry, 2018
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

open access: yes, 2008
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

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