✦ LIBER ✦

Effects of arginine density on the membrane-bound structure of a cationic antimicrobial peptide from solid-state NMR

✍ Scribed by Ming Tang; Alan J. Waring; Mei Hong

Book ID: 116274746
Publisher: Elsevier Science
Year: 2009
Tongue: English
Weight: 758 KB
Volume: 1788
Category: Article
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2008.10.027

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Arginine Dynamics in a Membrane-Bound Ca

Arginine Dynamics in a Membrane-Bound Cationic Beta-Hairpin Peptide from Solid-State NMR

✍ Ming Tang; Alan J. Waring; Mei Hong 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 316 KB

## Abstract The site‐specific motion of Arg residues in a membrane‐bound disulfide‐linked antimicrobial peptide, protegrin‐1 (PG‐1), was investigated by using magic‐angle‐spinning solid‐state NMR spectroscopy to better understand the membrane insertion and lipid interaction of this cationic membran

Effects of Guanidinium–Phosphate Hydroge

Effects of Guanidinium–Phosphate Hydrogen Bonding on the Membrane-Bound Structure and Activity of an Arginine-Rich Membrane Peptide from Solid-State NMR Spectroscopy

✍ Ming Tang; Alan J. Waring; Robert I. Lehrer; Mei Hong 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 509 KB

under 4.5 kHz MAS. Two-dimensional LG-CP and DIPSHIFT experiments were used to measure CÀH dipolar couplings and the ROCSA experiment was used to measure the 13 C NMR CSA values. Further details of orientation simulations are given in the Supporting Information.

Effects of Guanidinium–Phosphate Hydroge

Effects of Guanidinium–Phosphate Hydrogen Bonding on the Membrane-Bound Structure and Activity of an Arginine-Rich Membrane Peptide from Solid-State NMR Spectroscopy

✍ Ming Tang; Alan J. Waring; Robert I. Lehrer; Mei Hong 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 509 KB

Membrane-Bound Dimer Structure of a β-Ha

Membrane-Bound Dimer Structure of a β-Hairpin Antimicrobial Peptide from Rotational-Echo Double-Resonance Solid-State NMR †

✍ Mani, R.; Tang, M.; Wu, X.; Buffy, J. J.; Waring, A. J.; Sherman, M. A.; Hong, M 📂 Article 📅 2006 🏛 American Chemical Society 🌐 English ⚖ 347 KB

Membrane-Bound Conformation and Topology

Membrane-Bound Conformation and Topology of the Antimicrobial Peptide Tachyplesin I by Solid-State NMR †

✍ Doherty, Tim; Waring, Alan J.; Hong, M. 📂 Article 📅 2006 🏛 American Chemical Society 🌐 English ⚖ 309 KB

Structure and dynamics of cationic membr

Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR

✍ Mei Hong; Yongchao Su 📂 Article 📅 2011 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 568 KB

## Abstract Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier