✦ LIBER ✦

Dynamics of Formation of a Helix–Turn–Helix Structure in a Membrane-Active Peptide: A Time-Resolved Spectroscopic Study

✍ Scribed by Mariano Venanzi; Emanuela Gatto; Gianfranco Bocchinfuso; Antonio Palleschi; Lorenzo Stella; Fernando Formaggio; Claudio Toniolo

Publisher: John Wiley and Sons
Year: 2005
Tongue: English
Weight: 119 KB
Volume: 7
Category: Article
ISSN: 1439-4227
DOI: 10.1002/cbic.200500271

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Active-Site Structure and Dynamics of Cy

Active-Site Structure and Dynamics of Cytochrome c Immobilized on Self-Assembled Monolayers—A Time-Resolved Surface Enhanced Resonance Raman Spectroscopic Study

✍ Daniel H. Murgida; Peter Hildebrandt 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 129 KB 👁 2 views

A pH-dependent variation in α-helix stru

A pH-dependent variation in α-helix structure of the S-peptide of ribonuclease A studied by Monte Carlo simulated annealing

✍ Takashi Nakazawa; Sumiko Ban; Yuka Okuda; Masato Masuya; Ayori Mitsutake; Yuko O 📂 Article 📅 2002 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 386 KB 👁 1 views

## Abstract Low‐energy conformations of the S‐peptide fragment (20 amino acid residues long) of ribonuclease A were studied by Monte Carlo simulated annealing. The obtained lowest‐energy structures have α‐helices with different size and location, depending distinctively on the ionizing states of ac

ChemInform Abstract: Time-Resolved in si

ChemInform Abstract: Time-Resolved in situ X-Ray Diffraction Study of MCM-41 Structure Formation from a Homogeneous Environment.

✍ Jiri Rathousky; Guenter Schulz-Ekloff; Jiri Had; Arnost Zukal 📂 Article 📅 2010 🏛 John Wiley and Sons ⚖ 33 KB 👁 2 views

Cover Picture: Secondary Structure, Dyna

Cover Picture: Secondary Structure, Dynamics, and Topology of a Seven-Helix Receptor in Native Membranes, Studied by Solid-State NMR Spectroscopy (Angew. Chem. Int. Ed. 3/2007)

✍ Manuel Etzkorn; Swetlana Martell; Ovidiu C. Andronesi; Karsten Seidel; Martin En 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 132 KB 👁 2 views

**__Membrane proteins__** can now be studied in their native environments by using high‐resolution solid‐state NMR spectroscopy. Techniques that probe rigid, mobile, and water‐exposed protein segments provide insight into the membrane‐embedded structure of sensory rhodopsin II from __Natronomonas ph

Conformational change from antiparallel

Conformational change from antiparallel β-sheet to α-helix in a series of depsipeptide, -(Leu-Leu-Lac)n-: Syntheses, spectroscopic studies, and crystal structures of Boc-Leu-Lac-OEt and Boc-(Leu-Leu-Lac)n-OEt (n = 1, 2)

✍ Hiroyuki Oku; Keiichi Yamada; Ryoichi Katakai 📂 Article 📅 2008 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 510 KB

## Abstract The depsipeptides Boc‐Leu‐Lac‐OEt (1) and Boc‐(Leu‐Leu‐Lac)~__n__~‐OEt (__n__ = 1, 2) (**2** and **3**, respectively) (Boc = __tert__‐butyloxycarbonyl, Lac = L‐lactic acid residue) has been synthesized and studied by crystallographic, CD spectroscopic, and ESI‐MS analyses. In the packin