Journal article
Framework model for DNA polymerases
Biochemistry (Easton), Vol.44(18), pp.6877-6888
05/10/2005
Handle:
https://hdl.handle.net/2376/114836
PMID: 15865433
Abstract
DNA polymerases are complex machines with both chemical and mechanical functions. Recent crystal structures, ensemble kinetics, and single-molecule investigations have helped to elucidate the main properties of several DNA polymerases, all of which share common structural elements and a common basic mechanism, despite wide variations in amino acid sequence. The framework model is intended to aid in the understanding of these common features (and differences). It defines a class of models that automatically incorporates most of what is known about DNA polymerases within a single theoretical structure so that it is easier to make comparisons between them and to generate detailed models for specific polymerases. The framework model has three main elements: (1) a set of four key variables that describe the important motions within the protein-DNA-nucleotide complex, (2) a complete set of conformational states for the protein-DNA-nucleotide system, and (3) an approximate potential energy surface that controls the motions and transition rates between states. As an example application, we use the general framework ideas to build a detailed model for the HIV reverse transcriptase that is consistent with existing data, and predicts force-velocity curves and stepping-statistics histograms that can be directly compared to experiment.
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Details
- Title
- Framework model for DNA polymerases
- Creators
- David J Keller - Molecular Machines Laboratory, Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131, USA. dkeller@unm.eduJames A Brozik
- Publication Details
- Biochemistry (Easton), Vol.44(18), pp.6877-6888
- Academic Unit
- Chemistry, Department of
- Publisher
- United States
- Grant note
- GM63808 / NIGMS NIH HHS
- Identifiers
- 99900547867101842
- Language
- English
- Resource Type
- Journal article