✦ LIBER ✦

Structural determinants of protein folding

✍ Scribed by Tse Siang Kang; R. Manjunatha Kini

Publisher: Springer
Year: 2009
Tongue: English
Weight: 506 KB
Volume: 66
Category: Article
ISSN: 1420-682X
DOI: 10.1007/s00018-009-0023-5

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Determination of protein folding kinetic

Determination of protein folding kinetic types using sequence and predicted secondary structure and solvent accessibility

✍ Hua Zhang; Tuo Zhang; Jianzhao Gao; Jishou Ruan; Shiyi Shen; Lukasz Kurgan 📂 Article 📅 2010 🏛 Springer 🌐 English ⚖ 492 KB

Intrinsically Stable Secondary Structure

Intrinsically Stable Secondary Structure Elements of Proteins: A Comprehensive Study of Folding Units of Proteins by Computation and by Analysis of Data Determined by X-ray Crystallography

✍ András Perczel; Imre Jákli; Imre G. Csizmadia 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 240 KB 👁 1 views

Experimental and computational studies o

Experimental and computational studies of determinants of membrane-protein folding

✍ Jie Liang 📂 Article 📅 2002 🏛 Elsevier Science 🌐 English ⚖ 115 KB

Recent experiments and analysis have demonstrated the important roles of hydrogen bonding and polar-polar interactions in driving transmembrane helix-helix association. Further details of the energetics of helix-helix association and interhelical packing geometry are being mapped out. Many sequence

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

Structural argument for N-terminal initi

Structural argument for N-terminal initiation of protein folding

✍ Nickolai Alexandrov 📂 Article 📅 1993 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 258 KB

Energetics of protein structure and fold

Energetics of protein structure and folding

✍ David P. Goldenberg; Thomas E. Creighton 📂 Article 📅 1985 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 930 KB

The available experimental data on the kinetics of unfolding and refolding of small proteins are reviewed. Excluding slow transitions in the unfolded protein due to cis- trans isomerization of peptide bonds, the rate-limiting transition state in both unfolding and refolding is concluded to be a high