Article (Scientific journals)
The hydrophobic effect in protein folding.
Lins, Laurence; Brasseur, Robert
1995In FASEB Journal, 9 (7), p. 535-40
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Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Lins, Laurence  ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Brasseur, Robert ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Language :
English
Title :
The hydrophobic effect in protein folding.
Publication date :
1995
Journal title :
FASEB Journal
ISSN :
0892-6638
eISSN :
1530-6860
Publisher :
Federation of American Societies for Experimental Biology, United States - Maryland
Volume :
9
Issue :
7
Pages :
535-40
535-40
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 25 June 2010

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