Reference : The hydrophobic effect in protein folding.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/63801
The hydrophobic effect in protein folding.
English
Lins, Laurence mailto [Université de Liège > > Gembloux Agro-Bio Tech >]
Brasseur, Robert mailto [Université de Liège > > Gembloux Agro-Bio Tech >]
1995
FASEB Journal
9
7
535-40
Yes (verified by ORBi)
International
0892-6638
[en] In this review of protein folding we consider the noncovalent interactions
existing between atoms or molecules at the molecular level. The electrostatic,
Van der Waals, hydrogen bonding, and hydrophobic interactions are described and
their contribution to protein conformation is discussed. The growing interest in
the hydrophobic effect arises from its importance in the protein folding process,
and a semiempirical simulation of the free energy of solvation is proposed. In
most proteins, the different forces we describe contribute to the stability of
the protein conformation in a complex way. However, in the case of the
apolipoproteins and cytochrome C551, the energetic contributions are easily
distinguished. For this reason, these proteins are used to illustrate the
importance of the different energy fields.
Researchers ; Professionals
http://hdl.handle.net/2268/63801

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