Academic Journal
1 Biophysical Journal, Volume 97 Supporting Material Tilt and Rotation Angles of a Transmembrane Model Peptide as Studied by Fluorescence Spectroscopy
| العنوان: | 1 Biophysical Journal, Volume 97 Supporting Material Tilt and Rotation Angles of a Transmembrane Model Peptide as Studied by Fluorescence Spectroscopy |
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| المؤلفون: | Andrea Holt, Rob B. M. Koehorst, Tania Rutters-meijneke, Michael H. Gelb, Dirk T. S. Rijkers, Marcus A. Hemminga, J. Antoinette Killian |
| المساهمون: | The Pennsylvania State University CiteSeerX Archives |
| المصدر: | http://download.cell.com/biophysj/mmcs/journals/0006-3495/piis0006349509013058.mmc1.pdf. |
| المجموعة: | CiteSeerX |
| الوصف: | Supplementary material S1 Calculation of the tilt and rotation angles Figure S1: Schematic drawing of the angles describing the orientation of a tilted transmembrane peptide in the membrane. The tilt angle τ describes the angle between the membrane normal and the helix axis and the rotation angle ρ describes the angle between the direction of tilt and the Cα-atom of Gly1 in WALP23 with respect to the helix axis. The geometry of a regular α-helix is defined by an increment along the helix axis of dhelix = 1.5 Å per amino acid and a turn around the helix axis of ρhelix = 100 ° per amino acid. The distance xpos of the labeled cysteine at position nlabel with respect to the reference residue (Gly1) at position nref along the helix axis can then be calculated by ()labelrefhelixpos nndx − =. The orientation of a tilted transmembrane peptide is described by the angle τ between the membrane normal and the helix axis and the rotation angle ρ describes the angle between the direction of tilt and the Cα-atom of the reference residue with respect to the helix axis along the helix axis (for definitions see Fig. S1). The position of the label in a tilted transmembrane peptide is then calculated by ( ) ( ) () ()ρρττ −−− = helixreflabellabelposlabel nndxx cossincos, where dlabel is the distance between the label and the helix axis. The peak positions of the HICTm state and the total hydrogen-bonded fractions were fitted using a Gaussian function |
| نوع الوثيقة: | text |
| وصف الملف: | application/pdf |
| اللغة: | English |
| Relation: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.529.307; http://download.cell.com/biophysj/mmcs/journals/0006-3495/piis0006349509013058.mmc1.pdf |
| الاتاحة: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.529.307 http://download.cell.com/biophysj/mmcs/journals/0006-3495/piis0006349509013058.mmc1.pdf |
| Rights: | Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
| رقم الانضمام: | edsbas.CF5B1D98 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |