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Titlebook: GTPases in Biology I; Burton F. Dickey,Lutz Birnbaumer Book 1993 Springer-Verlag Berlin Heidelberg 1993 Calcium.DNA.Nucleotide.RNA.biochem

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Conformational Switch and Structural Basis for Oncogenic Mutations of , Proteins an approximate molecular mass of 21 kDa, and are hence named p21. Three . genes have been identified in human cells, H-., K-., and N-., and they all show a high degree of sequence homology for the first 165 amino acids, after which the sequences diverge. The p21 proteins are attached to the cytopla
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Analysis of Ras Structure and Dynamics by Nuclear Magnetic Resonance proteins which are located on the inner surface of the plasma membrane. They are believed to function as signal switch molecules which relay extracellular growth promoting signals to intracellular targets by cycling between the biologically active ras.GTP and the inactive ras.GDP forms. The on (ras
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Molecular Dynamics Studies of H-, p21-GTP of the method is the development of a potential energy surface, or “force field”, from which the forces on all atoms of the system can be derived. This force field is typically parameterized by resorting to spectroscopic methods and ab initio quantum mechanical computations on smaller molecules. On
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Proofreading in the Elongation Cycle of Protein Synthesise P site of the ribosome (Fig. 1b). Translocation is also accompanied by GTP hydrolysis, with EF-G-GDP being released from the ribosome. The third elongation factor, EF-Ts, catalyzes the exchange of GTP for GDP on EF-Tu.
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