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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1979-1-15
|
| pubmed:abstractText |
Differential enthalpies (deltaH) and entropies (deltaS) of the interaction of water with a high and low temperature conformer of alpha-chymotrypsin were determined previously by multitemperature sorption measurements. The changes in (deltaH) and (deltaS) with water content of the protein were found to show a pronounced compensation pattern. It is known that van 't Hoff data may exhibit enthalpy-entropy compensation, which is entirely due to statistical error propagation. To discriminate between artifactual and significant compensation, the experimental results are analyzed by statistical methods. The results of two different statistical analyses show that a linear, chemically caused compensation effect can be established for the interaction of water with both chymotrypsin conformers. The compensation temperature beta = deltaH/deltaS was found to be 433 +/- 22 K. The compensation effect is detectable only in the water content range above the monolayer volume (upsilonm), computed by the Brunauer, Emmett and Teller equation. This result is discussed in terms of a monolayer hydration mechanism, formulated on the basis of previous thermodynamic results: The interaction of the first water monolayer with the charged and polar surface area of the dry protein, largely stabilizes its tertiary structure. Further water addition then occurs to a practically invariable protein surface. According to this mechanism (which ensures a maximum of conformational stability with a minimum of hydration water), large conformational changes can be expected to occur mainly in the monolayer water content range. This expectation is confirmed by extra-thermodynamic data (infrared and X-ray measurements). The thermodynamic quantities of the sorption process are thus governed by conformational effects below upsilonm. Above the monolayer water content range, however, the water binding process per se strongly predominates. The deltaH/deltaS compensation effect established for this water content range, is thus attributable to phase transitions of water molecules from the gas (or liquid) phase to the protein-bound state (or vice versa). A possible relationship between the linear compensation effect established in this study, and the compensation phenomenon observed in reactions in aqueous solution is discussed.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
26
|
| pubmed:volume |
536
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
27-37
|
| pubmed:dateRevised |
2000-12-18
|
| pubmed:meshHeading |
pubmed-meshheading:708766-Calorimetry,
pubmed-meshheading:708766-Chymotrypsin,
pubmed-meshheading:708766-Hydrogen Bonding,
pubmed-meshheading:708766-Protein Binding,
pubmed-meshheading:708766-Protein Conformation,
pubmed-meshheading:708766-Temperature,
pubmed-meshheading:708766-Thermodynamics,
pubmed-meshheading:708766-Water
|
| pubmed:year |
1978
|
| pubmed:articleTitle |
Thermodynamic studies of the interaction of alpha-chymotrypsin with water. II. Statistical analyses of the enthalpy-entropy compensation effect.
|
| pubmed:publicationType |
Journal Article
|