Many adhesive proteins present in extracellular matrices and in blood contain the tetrapeptide sequence -Arg-Gly-Asp-Ser-(or RGDS) at their cell recognition site. Since this sequence, or similar ones, was found in many proteins involved in major biological mechanisms, conformational investigations w
✦ LIBER ✦
Computer simulation of the conformational behaviour of angiotensinogen (6–13) renin substrate
✍ Scribed by M. Benkoulouche; M. Cotrait; B. Maigret
- Publisher
- Springer Netherlands
- Year
- 1992
- Tongue
- English
- Weight
- 603 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0920-654X
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✦ Synopsis
The conformational behaviour of the biologically active angiotensinogen (6-13) fragment has been investigated by computer simulations. A large sample of conformers has been generated using the Monte-Carlo procedure, then analysed using classification and partition methods. Seven families can describe the conformational distribution. About 40% of conformers are fully extended, 28% are folded at the C-terminal His 6-Pro7-PheS-His 9 level and the others are folded at different levels. The study highlights the extreme flexibility of the angiotensinogen fragment.
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