NMR studies on partially folded and unfolded states of metalloproteins
β Scribed by Paola Turano
- Book ID
- 108403814
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 250 KB
- Volume
- 96
- Category
- Article
- ISSN
- 0162-0134
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Studies of unfolded and partially folded proteins provide important insight into the initiation and process of protein folding. This review focuses on the use of nmr in characterization of ensembles of proteins that model the early stages of folding. Analysis of an ensemble includes description of t
It has been shown that human stefin B exhibits molten globule intermediates when denatured by acid or GuHCl. In the presence of TFE, it transforms into a highly helical state. In our first study on its folding mechanism (Z Λerovnik et al., Proteins 32:296-303), the kinetics measured by circular dich
The backbone 'H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter protein, drk, have been assigned. This domain is in slow exchange on the NMR timescale between folded and predominantly unfolded states. Data were collected on both states simultaneously, on samples o
## Abstract A threeβdimensional lattice model of protein designed to assimilate lysozyme is introduced. An attractive interaction is assumed to work between preassigned specific pairs of units, when they occupy the nearestβnighbor lattice points. The behavior of this lattice lysozyme is studied by