New PDF release: Group Theory and Solid State Physics

By Mariot L.

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If, on the other hand, it equals to half the weight of the molecule this proves that there are two binding sites per molecule and so on. In anticipation of the findings to be related further on suffice is to say that the dimer of tubulin weighs 110,000 daltons, and that it is composed of one monomer of α-tubulin and one monomer of β-tubulin, each weighing 55,000 daltons. Considering that a binding experiment with pure tubulin finds the equivalent binding-weight for colchicine to be appr. 110,000 daltons and that for guanosine-triphosphate (GTP) to be appr.

Nature 375:424–427 Nogales E, Downing KH, Amos LA, Löwe J (1998a) Tubulin and FtsZ form a distinct family of GTPases. Nat struct Biol 5:451–458 Nogales E, Wolf SG, Downing KH (1998b) Structure of the αβ tubulin dimer by electron crystallography. Nature 391:199–203 Oesterhelt D, Stoeckenius W (1971) Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat New Biol 233:149–152 Pennisi E (1998) Structure of Key cytoskeletal protein tubulin revealed. Science 279:176–177 Penrose R (1994) Shadows of the mind.

In its ring forms a hexose, again, can exist either as a furanose, a five-member ring, or as a pyranose, a six-membered ring. Both these rings can assume different conformations, especially when bulky groupings are attached to them. While the different conformations, 24 of them, of the unsubstituted hexose in the furanose form are energetically nearly equivalent, a hexose in the pyranose form will exist in one or a few of the energetically preferable conformations the so called chair and boat forms of the molecule.

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Group Theory and Solid State Physics by Mariot L.

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