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كتاب Frederix P L T M Hoogenboom B W Fotiadis D Atomic Force Microscopy of Biological Samples لD Fotiadis D J Müller and A Engel

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التصنيف : كتب منوعة
الفئة : Biology Books
سنة النشر : 2004
عدد الصفحات : غير محدد
عن الكتاب : 2004م - 1443هـ نبذه عن الكتاب: lied to the stylus was approximately 50 pN, preventing a force-induced conformational change of the E–F loop. This loop is known to deform when the force is increased to 100 pN, thereby changing the conformation of the bR surface.15 Interestingly, observations of different atomic models from x-ray crystallography show that the variation of this region is pronounced: the E–F loop is involved in the contacts leading to the 3D crystals, and its conformation is dictated by the 3D packing arrangement of the bR molecules. Although all the bR trimers are identical in the 2D crystal displayed in Figure 3a, their surface structure varies significantly. These changes are related to the flexibility of the bR surface rather than any noise introduced by the AFM. The flexibility of the surface lowers the resolution of the ensemble, but structural details of each trimer are still discernable. The variations in the trimer structure can be used to calculate the probability of finding a certain loop at a certain position (x,y) by mapping the corresponding peak positions of all individual bR trimers.16 The E–F loop, which exhibits significant flexibility, is more delocalized than the A–B loop, which occupies a more defined position. The signal about the threefold axis results from a lipid molecule protruding 0.1 nm, which is only occasionally visible in the raw data, but if present, is precisely localized in the center of the trimer. Therefore, a strong signal emerges in the probability map (Figure 3c), whereas no signal is present in the average (Figure 3b). Precise localization of a surface feature suggests that the correspondin .
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نبذة عن كتاب Frederix P L T M Hoogenboom B W Fotiadis D Atomic Force Microscopy of Biological Samples

كتاب Frederix P L T M Hoogenboom B W Fotiadis D Atomic Force Microscopy of Biological Samples

2004م - 1443هـ نبذه عن الكتاب: lied to the stylus was approximately 50 pN, preventing a force-induced conformational change of the E–F loop. This loop is known to deform when the force is increased to 100 pN, thereby changing the conformation of the bR surface.15 Interestingly, observations of different atomic models from x-ray crystallography show that the variation of this region is pronounced: the E–F loop is involved in the contacts leading to the 3D crystals, and its conformation is dictated by the 3D packing arrangement of the bR molecules. Although all the bR trimers are identical in the 2D crystal displayed in Figure 3a, their surface structure varies significantly. These changes are related to the flexibility of the bR surface rather than any noise introduced by the AFM. The flexibility of the surface lowers the resolution of the ensemble, but structural details of each trimer are still discernable. The variations in the trimer structure can be used to calculate the probability of finding a certain loop at a certain position (x,y) by mapping the corresponding peak positions of all individual bR trimers.16 The E–F loop, which exhibits significant flexibility, is more delocalized than the A–B loop, which occupies a more defined position. The signal about the threefold axis results from a lipid molecule protruding 0.1 nm, which is only occasionally visible in the raw data, but if present, is precisely localized in the center of the trimer. Therefore, a strong signal emerges in the probability map (Figure 3c), whereas no signal is present in the average (Figure 3b). Precise localization of a surface feature suggests that the correspondin .


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