✦ LIBER ✦

Discrimination of the native from misfolded protein models with an energy function including implicit solvation

✍ Scribed by Themis Lazaridis; Martin Karplus

Book ID: 115629248
Publisher: Elsevier Science
Year: 1999
Tongue: English
Weight: 215 KB
Volume: 288
Category: Article
ISSN: 0022-2836
DOI: 10.1006/jmbi.1999.2685

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Discrimination of near-native protein st

Discrimination of near-native protein structures from misfolded models by empirical free energy functions

✍ David W. Gatchell; Sheldon Dennis; Sandor Vajda 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 552 KB

Free-energy function for discriminating

Free-energy function for discriminating the native fold of a protein from misfolded decoys

✍ Satoshi Yasuda; Takashi Yoshidome; Yuichi Harano; Roland Roth; Hiraku Oshima; Ko 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 688 KB

## Abstract In this study, free‐energy function (FEF) for discriminating the native fold of a protein from misfolded decoys was investigated. It is a physics‐based function using an all‐atom model, which comprises the hydration entropy (HE) and the total dehydration penalty (TDP). The HE is calcula

Discrimination between native and intent

Discrimination between native and intentionally misfolded conformations of proteins: ES/IS, a new method for calculating conformational free energy that uses both dynamics simulations with an explicit solvent and an implicit solvent continuum model

✍ Yury N. Vorobjev; Juan Carlos Almagro; Jan Hermans 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 179 KB 👁 3 views

A new method for calculating the total conformational free energy of proteins in water solvent is presented. The method consists of a relatively brief simulation by molecular dynamics with explicit solvent (ES) molecules to produce a set of microstates of the macroscopic conformation. Conformational