Properties of the protein matrix revealed by the free energy of cavity formation.
| Data(s) |
01/12/1996
|
|---|---|
| Resumo |
The classical picture of the hydrophobic stabilization of proteins invokes a resemblance between the protein interior and nonpolar solvents, but the extent to which this is the case has often been questioned. The protein interior is believed to be at least as tightly packed as organic crystals, and was shown to have very low compressibility. There is also evidence that these properties are not uniform throughout the protein, and conflicting views exist on the nature of sidechain packing and on its influence on the properties of the protein. Journal Article Research Support, Non-U.S. Gov't info:eu-repo/semantics/published |
| Formato |
1 full-text file(s): application/pdf |
| Identificador |
uri/info:pmid/8994976 https://dipot.ulb.ac.be/dspace/bitstream/2013/79660/1/Properties-protein-matrix-free-energy.pdf http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/79660 |
| Idioma(s) |
en |
| Direitos |
1 full-text file(s): info:eu-repo/semantics/openAccess |
| Fonte |
Structure, 4 (12 |
| Palavras-Chave | #Chimie #Thermodynamics #fording #hydrophobic interactions #sidechain packing #stability |
| Tipo |
info:eu-repo/semantics/article info:ulb-repo/semantics/articlePeerReview info:ulb-repo/semantics/openurl/article |
