The chain dynamics of the tetradecapeptide mastoparan bound to calcium-saturated calmodulin have been studied using inelastic and quasielastic neutron scattering measurements. Two broad peaks were observed in the difference TOF spectrum and were assigned on the basis of the structure of mastoparan,
The Main Chain Dynamics of a Peptide Bound to Calmodulin
✍ Scribed by C. Chen; Y.Q. Feng; J.H. Short; A.J. Wand
- Book ID
- 115564717
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 408 KB
- Volume
- 306
- Category
- Article
- ISSN
- 0003-9861
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Tb(III) luminescence is used to probe the conformational change induced in the calcium regulatory protein calmodulin upon binding to a target peptide. The luminescence lifetime for Tb(III) measured by frequency domain fluorimetry increases from 1278 microseconds for the calmodulin complex to 1496 mi
X-Ray diffraction analysis of the model peptide Boc-Thr-Thr-OCH 3 reveals the existence of distinctive conformational characteristics: semi-extended (=-62.1°; =137.1°) and semi-folded (=-130.3°; T =5.7°) of the N-and C-terminus Thr residues, respectively. Surprisingly, an overall significantly 'flat