Resolving pathways of functional coupling within protein assemblies by site-specific structural perturbation
| Autor: | Gary K. Ackers, Francine R. Smith |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Macromolecular Substances
Protein subunit Hemoglobins Abnormal 030303 biophysics Mutant Kinetics Biophysics Structural perturbation 03 medical and health sciences chemistry.chemical_compound Hemoglobins Native protein Humans Amino acid residue Heme 030304 developmental biology 0303 health sciences Chemistry Chemical modification Proteins Biochemistry Thermodynamics Protein Processing Post-Translational Research Article |
| Zdroj: | Biophysical Journal. 49(1):155-165 |
| ISSN: | 0006-3495 |
| DOI: | 10.1016/s0006-3495(86)83631-1 |
| Popis: | Site-specific structural modification is a powerful tool for studying functional mechanisms in proteins where the structures may be manipulated by direct chemical modification, by selection of naturally-occurring mutants, or by site-directed mutagenesis. Here, we present a general strategy for such studies, which we term "mapping by structure-function perturbation." A series of functional perturbations (i.e., deviations of functional behavior from that of the native protein) are mapped against the structural locations of the modified sites, obtained over a range of locations. The modifications are treated as arbitrary perturbations of structure at specific locations, in contrast to the conventional approach of trying to interpret their local stereochemistry. The map yields information on structural locations of functional events and pathways of coupling within protein assemblies. We have applied this approach to the ligand-linked subunit assembly of human hemoglobin, using both chemically-modified heme sites (CN-met), and amino acid residues altered by mutation and chemical modification. |
| Databáze: | OpenAIRE |
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