𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Residue-Specific Side-Chain Packing Determines the Backbone Dynamics of Transmembrane Model Helices

✍ Scribed by Quint, Stefan; Widmaier, Simon; Minde, David; Hornburg, Daniel; Langosch, Dieter; Scharnagl, Christina

Book ID
119207516
Publisher
Biophysical Society
Year
2010
Tongue
English
Weight
669 KB
Volume
99
Category
Article
ISSN
0006-3495

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Peptide models. XIV. Ab initio study on
Peptide models. XIV. Ab initio study on the role of side-chain backbone interaction stabilizing the building unit of right- and left-handed helices in peptides and proteins
✍ András Perczel; Ödön Farkas; John F. Marcoccia; Imre G. Csizmadia 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 407 KB 👁 2 views

Previous ab initio computations revealed that the conformational building unit of the Ž . right-handed helix f y54Њ, f y45Њ is not an energy minimum on two-Ž Ä 4 . dimensional-type Ramachandran potential energy surfaces E s E , . Theoretical investigations were performed on several single-amino-acid

Determination of side-chain-rotamer and
Determination of side-chain-rotamer and side-chain and backbone virtual-bond-stretching potentials of mean force from AM1 energy surfaces of terminally-blocked amino-acid residues, for coarse-grained simulations of protein structure and folding. I. The method
✍ Urszula Kozłowska; Adam Liwo; Harold A. Scheraga 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 381 KB 👁 1 views

## Abstract In this and the accompanying article, we report the development of new physics‐based side‐chain‐rotamer and virtual‐bond‐deformation potentials which now replace the respective statistical potentials used so far in our physics‐based united‐reside UNRES force field for large‐scale simula