High impact information on Protein Footprinting

• Evidence that Region I senses the conformation of the promoter was obtained from protein footprint experiments [1].
• The complex was subjected to protein footprinting and the results implicated an RNP1-like sequence and a sequence region immediately N-terminal to a putative leucine zipper in substrate binding [2].
• The molecular basis for the pituitary-specific expression of the human growth hormone (hGH) gene was investigated, by gene transfer and protein footprinting experiments [3].
• Protein footprinting at cysteines: probing ATP-modulated contacts in cysteine-substitution mutants of yeast DNA topoisomerase II [4].
• In this work, we have used hydroxyl-radical protein footprinting to define determinants of alpha for interaction with beta, beta', and sigma [5].

Biological context of Protein Footprinting

• Hydroxyl radical protein footprinting and alanine-scanning mutagenesis were used to investigate the interactions of GreB with RNA polymerase alone and in a ternary elongation complex [6].
• The erythroid binding protein NF-E1 and a ubiquitous octamer protein footprint the -195 to -170 site [7].
• The IE2 protein footprint was between bp -15 and +2, relative to the transcription start site, and the cellular protein was between bp -16 and +7 [8].
• Thus, protein footprinting with DZN emerges as a feasible methodology useful for mapping contact regions of protein domains involved in macromolecular assemblies [9].

Associations of Protein Footprinting with chemical compounds

• A two-step lysine-modification procedure has been devised to chemically footprint protein surfaces involved in macromolecular interactions [10].
• Fluorescence-based protein footprinting using histidine-tagged protein [11].

Gene context of Protein Footprinting

• In this work, we employed a mass spectrometric protein footprinting method of single amino acid resolution to investigate the interactions of the entire heterotrimeric hRPA with ssDNA [12].
• Protein footprinting data suggest that Rev interacts specifically with amino acids within the 196-208 region of p32 [13].
• A series of N-terminal, C-terminal, and internal deletion mutants, as well as protein footprinting, were used to identify the target regions in GAD65 [14].
• Protein footprinting analysis, whereby polypeptide fragments generated on protease treatment of immune complexes are studied, indicated considerable heterogeneity in antibody recognition of IA-2, even between sera with similar reactivity to deletion mutants [15].
• Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting [16].

References