𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Solvent accessible surface area approximations for rapid and accurate protein structure prediction

✍ Scribed by Elizabeth Durham; Brent Dorr; Nils Woetzel; René Staritzbichler; Jens Meiler

Book ID
106240039
Publisher
Springer-Verlag
Year
2009
Tongue
English
Weight
492 KB
Volume
15
Category
Article
ISSN
1610-2940

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Maintaining solvent accessible surface a
Maintaining solvent accessible surface area under rotamer substitution for protein design
✍ Andrew Leaver-Fay; Glenn L. Butterfoss; Jack Snoeyink; Brian Kuhlman 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 125 KB

## Abstract Although quantities derived from solvent accessible surface areas (SASA) are useful in many applications in protein design and structural biology, the computational cost of accurate SASA calculation makes SASA‐based scores difficult to integrate into commonly used protein design methodo

SPINE X: Improving protein secondary str
SPINE X: Improving protein secondary structure prediction by multistep learning coupled with prediction of solvent accessible surface area and backbone torsion angles
✍ Eshel Faraggi; Tuo Zhang; Yuedong Yang; Lukasz Kurgan; Yaoqi Zhou 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 154 KB

## Abstract Accurate prediction of protein secondary structure is essential for accurate sequence alignment, three‐dimensional structure modeling, and function prediction. The accuracy of __ab initio__ secondary structure prediction from sequence, however, has only increased from around 77 to 80% o

Efficient approximate all-atom solvent a
Efficient approximate all-atom solvent accessible surface area method parameterized for folded and denatured protein conformations
✍ Olgun Guvench; Charles L. Brooks III 📂 Article 📅 2004 🏛 John Wiley and Sons 🌐 English ⚖ 485 KB

## Abstract Continuing advances in computer hardware and software are permitting atomic‐resolution molecular simulations for longer time scales and on larger systems. Despite these advances, routinely performing atomistic simulations with explicit water for even small proteins, which reach the fold

A sequence-based computational model for
A sequence-based computational model for the prediction of the solvent accessible surface area for α-helix and β-barrel transmembrane residues
✍ Chengqi Wang; Lili Xi; Shuyan Li; Huanxiang Liu; Xiaojun Yao 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 816 KB

## Abstract Predicting the solvent accessible surface area (ASA) of transmembrane (TM) residues is of great importance for experimental researchers to elucidate diverse physiological processes. TM residues fall into two major structural classes (α‐helix membrane protein and β‐barrel membrane protei