Mapping hydration dynamics around a protein surface
Picosecond
Protein Dynamics
Globular protein
Dynamics
Surface protein
DOI:
10.1073/pnas.0707647104
Publication Date:
2007-11-15T02:19:01Z
AUTHORS (7)
ABSTRACT
Protein surface hydration is fundamental to its structure and activity. We report here the direct mapping of global dynamics around a protein in native molten globular states, using tryptophan scan by site-specific mutations. With 16 mutants 29 different positions we observed two robust, distinct water layer on few ( approximately 1-8 ps) tens hundreds picoseconds 20-200 ps), representing initial local relaxation subsequent collective network restructuring, respectively. Both time scales are strongly correlated with protein's structural chemical properties. These results reveal intimate relationship between fluctuations such biologically relevant water-protein interactions fluctuate picosecond scales.
SUPPLEMENTAL MATERIAL
Coming soon ....
REFERENCES (47)
CITATIONS (297)
EXTERNAL LINKS
PlumX Metrics
RECOMMENDATIONS
FAIR ASSESSMENT
Coming soon ....
JUPYTER LAB
Coming soon ....