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Obtaining protein solvent accessible surface area when structural data is unavailable using osmotic pressure
Author(s) -
Mc Bride Devin W.,
Rodgers V. G. J.
Publication year - 2012
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.12648
Subject(s) - sasa , accessible surface area , chemistry , solvent , osmotic pressure , monomer , hemoglobin , aggregate (composite) , thermodynamics , materials science , computational chemistry , nanotechnology , biochemistry , biology , botany , organic chemistry , physics , polymer
Here, we provide an algorithm that predicts solvent accessible surface area (SASA) using concentrated solution osmotic pressure data. Sheep hemoglobin monomer and β‐lactoglobulin are used for verification. Additionally, SASA for structurally unknown calf lens α‐crystallin aggregate is predicted. Using osmotic pressure data, the predicted SASA value for sheep hemoglobin, 22,398 ± 1,244 Å 2 , was in excellent agreement with computational model predictions (24,304 Å 2 ‐26,100 Å 2 ). Similarly, predicted SASA values for bovine β‐lactoglobulin in pH solutions of pH 5.1, 6.0, and 8.0, were 5,765 ± 1,031 Å 2 , 6,656 ± 1,082 Å 2 , and 9,141 ± 1,060 Å 2 , respectively, were in good agreement with the computationally determined SASA value (7,500 Å 2 –8,628 Å 2 ). Predicted SASA for the aggregate of calf lens α‐crystallin (800 kDa) was found to be 417,691 ± 16,790 Å 2 . These results illustrate that this novel method can provide an important experimental alternative in estimating SASA for proteins and, possibly, their complexes in solution. © 2011 American Institute of Chemical Engineers AIChE J, 2012