title: Steric constraints dependent on nucleobase pair orientation vary in different DNA polymerase active sites.
abstract: Finding the right fit: Herein, we report on the development of novel steric probes and present initial insights into their interplay with DNA polymerases. Our findings provide experimental evidence for varied enzyme-substrate interactions that might account for the varied selectivity previously observed.
authors: Department of Chemistry, and Konstanz Research School Chemical Biology, Universität Konstanz, Universitätsstrasse 10, Konstanz, Germany.
authors: Frank
authors: F
authors: Streckenbach
authors: Gopinath
authors: G
authors: Rangam
authors: Heiko M
authors: HM
authors: Möller
authors: Andreas
authors: A
authors: Marx
mesh_terms: D020029:Base Pairing; D020134:Catalytic Domain; D004256:DNA Polymerase I / Q000737:chemistry* / Q000378:metabolism; D019951:DNA Polymerase beta / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D009711:Nucleotides / Q000737:chemistry*; D013379:Substrate Specificity
chemical_list: D009711:Nucleotides; D004256:DNA Polymerase I; D019951:DNA Polymerase beta