Other Publications (1)
Articles by Natalie A. LaFranzo in JoVE
Creating Two-Dimensional Patterned Substrates for Protein and Cell Confinement Dawn M. Johnson1, Natalie A. LaFranzo1, Joshua A. Maurer1 1Department of Chemistry, Washington University in St. Louis Self-assembled monolayers (SAMs) formed from long chain alkane thiols on gold provide well-defined substrates for the formation of protein patterns and cell confinement. Microcontact printing of hexadecanethiol using a polydimethylsiloxane (PDMS) stamp followed by backfilling with a glycol-terminated alkane thiol monomer produces a pattern where protein and cells adsorb only to the stamped hexadecanethiol region.
Other articles by Natalie A. LaFranzo on PubMed
Sequence or Structure: Using Bioinformatics and Homology Modeling to Understand Functional Relationships in CAMP/cGMP Binding Domains Molecular BioSystems. May, 2010 | Pubmed ID: 20567776 The relationship between sequence, structure, and function is examined by comparing nineteen cyclic nucleotide monophosphate binding domains of known structure from six different functional families. Comparisons are made by structure and sequence alignment and through the generation of 3610 homology models. This analysis suggests there are only weak relationships between functional families, sequence, and/or structure. However, we have identified that for cyclic nucleotide monophosphate binding domains privileged template structures occur for homology modeling. The existence of privileged template structures, capable of creating accurate modeling for a broad family of proteins, may lead to improved homology modeling protocols.