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Chemical Approaches to the Analysis of Ribosome Architecture

Gary R. Craven, Brian Rigby, Li-Ming Changchien


The present state of knowledge of ribosome structure bears a clear resemblance to the problem of enzyme structures as it developed prior to the impact of X-ray crystallography. During that period investigators utilized virtually any techniques they could imagine to uncover the fine details of protein architecture. One of the most widely applied methods to obtain significant information about protein structure has been the utilization of chemicals capable of selectively derivatizing polypeptide side chains. Over the years a substantial number of these reagents have been studied for their ability to react more or less selectively with amino acid functional groups. These reagents are used to determine which amino acid side groups are involved in the function of the enzyme and also to differentiate between so-called “buried” and “exposed” side chains. These data, combined with primary sequence information, have yielded considerable general knowledge of the three-dimensional structure of numerous proteins.

Application of Protein Modifying Reagents to the Problem of Ribosome Structure
A number of workers have attempted to extend the use of chemical reagents to determine some general features of ribosome structure (Acharya and Moore 1973; Craven and Gupta 1970; Ginzburg, Miskin and Azmir 1973; Huang and Cantor 1972; Hsiung and Cantor 1973; Kahan and Kaltschmidt 1972; Michalski, Sells and Morrison 1973; Miller and Sypherd 1973; Visentin, Yaguchi and Kaplan 1973). The initial effort with ribosomes has been to search for some gross reflections of protein organization within the ribosome architecture. Thus a fair number of different protein reagents have...

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