Volume 272, Number 2, Issue of January 10, 1997 pp. 699-699
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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MINIREVIEW:
Protein Folding and Assembly Minireview Series^*

From the Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005-1892

INTRODUCTION

FOOTNOTES

INTRODUCTION

In this issue we begin a five-part minireview series that addresses topics in protein folding and assembly, an area of keen interest in biochemistry and molecular biology. Whether attempting to predict structure from DNA sequences, dealing with insolubility of proteins expressed in bacterial cells, exploring structure/function relationships in specific proteins, or directly examining issues in protein folding, this series addresses issues of import in this rapidly expanding and relevant field. This week Ken Dill examines additivity principles in protein structure determination and argues that traditional models for thermodynamic additivity and independence may, of necessity, give way to statistical mechanical models and molecular dynamics simulations for generating predictive theories. Next week, George Rose presents a cogent argument for local entropically driven segments of emerging secondary structure, in particular -helices, providing the framework for subsequent protein folding. In the ensuing three weeks, Michael Hecht will examine the key issues in de novo protein design, providing guidance for the choices of de novo sequences in this process of growing importance both to industrial and basic research efforts; Robert Hodges presents a detailed review of the multiplicity of -helical assembly motifs in a wide variety of proteins; and Raymond Ruddon explores the process of protein folding in vivo and the requirement for "assistance" in achieving rapid folding rates in the cellular context. In this series, we have attempted to integrate multiple aspects of protein folding/assembly and to present a summary that will provide facile access to the vast literature in this extensive enterprise.

FOOTNOTES