Download Computer Assisted Modeling: Contributions of Computational by National Research Council, Division on Earth and Life PDF

By National Research Council, Division on Earth and Life Studies, Commission on Life Sciences, Committee on Computer-Assisted Modeling

Normal Books e-book date: 2009 unique ebook date: 1987 unique writer: nationwide Academies unique Identifier: NAP:13431 topics: laptop simulation Macromolecules pcs / normal know-how

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Additional resources for Computer Assisted Modeling: Contributions of Computational Approaches to Elucidating Macromolecular Structure and Function

Example text

For example, a program can provide the calculated lowest free energy structure, as well as other significantly different low free energy structures (Williams and Tinoco, 1986). Experiments are done to test some of the predicted substructures, and their results are incorporated into the calculation of the next prediction. , 1983). Computer methods of the future must be based on much more detailed knowledge of the thermodynamics of local regions of an RNA molecule. The extensive thermodynamic data needed for correct prediction of secondary structure will most likely come from computer interpolation and extrapolation of limited data measured on synthetic oligonucleotides in a few solvents.

TERTIARY STRUCTURE OF PROTEINS AND NUCLEIC ACIDS: EXPERIMENTAL 41 5. Tertiary Structure of Proteins and Nucleic Acids: Experimental X-RAY DIFFRACTION OF BIOLOGICAL MACROMOLECULES In 1934 Bernal and Crowfoot demonstrated that a crystalline protein could give rise to a well-ordered x-ray diffraction pattern, thus setting the stage for modern analysis of the structure of proteins. , 1954). The culmination of these years of work came in 1959 when Kendrew and his colleagues (1960) reported the analysis of myoglobin at 2 Å resolution, revealing for the first time the underlying structure of a globular protein.

Because the map is of less-than-atomic resolution and also contains errors in the phase determination, the investigator must have considerable skill to obtain the best fit. The resulting protein model must then be refined to remove the errors present in the map as much as possible as well as those errors introduced by the fitting process. Computers play an essential role in most of these steps. Even the analyses of the first protein crystal structure, myoglobin, could not have been accomplished without the use of the EDSACII in Cambridge (Kendrew, 1960).

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