๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Improvement of the relative entropy based protein folding method

โœ Scribed by LiSheng Qi; JiGuo Su; WeiZu Chen; CunXin Wang


Publisher
Science in China Press (SCP)
Year
2009
Tongue
English
Weight
589 KB
Volume
52
Category
Article
ISSN
1672-1799

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


On the entropy of protein folding
โœ George I. Makhatadze; Peter L. Privalov ๐Ÿ“‚ Article ๐Ÿ“… 2008 ๐Ÿ› Cold Spring Harbor Laboratory Press ๐ŸŒ English โš– 484 KB

## Abstract The failure to appreciate that the hydration of polar groups is a major contribution to the entropy of protein unfolding has led to considerable underestimates for the loss of configurational freedom when a protein chain folds.

A method for the improvement of threadin
โœ Andrzej Kolinski; Piotr Rotkiewicz; Bartosz Ilkowski; Jeffrey Skolnick ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 627 KB

A new method for the homologybased modeling of protein three-dimensional structures is proposed and evaluated. The alignment of a query sequence to a structural template produced by threading algorithms usually produces lowresolution molecular models. The proposed method attempts to improve these mo

Estimates of the loss of main-chain conf
โœ Debnath Pal; Pinak Chakrabarti ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 100 KB ๐Ÿ‘ 2 views

The average contribution of conformational entropy for individual amino acid residues towards the free energy of protein folding is not well understood. We have developed empirical scales for the loss of the main-chain (torsion angles, and ) conformational entropy by taking its side-chain into accou