We outline a general strategy for determining the effective coarse-grained interactions between the amino acids of a protein from the experimentally derived nativestate structures. The method is, in principle, free from any adjustable or empirically determined parameters, and it is tested on simple
β¦ LIBER β¦
Protein Folding by Interaction
β Scribed by Buchner, Johannes; Kessler, Horst
- Book ID
- 125803553
- Publisher
- Elsevier Science
- Year
- 2014
- Tongue
- English
- Weight
- 198 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0969-2126
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Interaction potentials for protein foldi
β
Flavio Seno; Amos Maritan; Jayanth R. Banavar
π
Article
π
1998
π
John Wiley and Sons
π
English
β 56 KB
π 2 views
Protein folding and interactions reveale
β
Alexander M Last; Carol V Robinson
π
Article
π
1999
π
Elsevier Science
π
English
β 213 KB
Mass spectrometry is capable of examining very large, dynamic proteins and this ability, coupled with its relatively high throughput and low sample requirements, is reflected by its increasing importance for the characterisation of protein structure. Recent developments in mass spectrometry, in part
Exploring protein interactions by intera
β
Stephen W Michnick
π
Article
π
2001
π
Elsevier Science
π
English
β 396 KB
Protein folding by stages
β
Jonathan J. Ewbank; Thomas E. Creighton
π
Article
π
1992
π
Elsevier Science
π
English
β 461 KB
Protein folding by numbers
β
Pain, Roger
π
Article
π
1982
π
Nature Publishing Group
π
English
β 269 KB
Entropy in protein folding and in protei
β
G Patrick Brady; Kim A Sharp
π
Article
π
1997
π
Elsevier Science
π
English
β 671 KB