Non covalent interactions in protein complexes (CROSBI ID 547817)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa
Podaci o odgovornosti
Tomić, Sanja ; Bertoša, Branimir ; Wade, C. Rebecca
engleski
Non covalent interactions in protein complexes
While the electrostatic interactions between the complementary charged proteins increase their interaction, desolvation of the charged and polar amino acid residues destabilizes the protein – protein complex. We studied influence of the electrostatic interactions on formation of the protein complexes between Ras and Rap and their effectors Raf and RalGDS. For this purpose we were solving the Poisson Boltzman equations using the Finite difference method as built in the program UHBD. The electrostatic contribution to desolvation is defined as loss of the electrostatic interaction between protein and solvent upon binding. The calculations revealed negative correlation between binding affinity and desolvation i.e the tightest complexes have the highest desolvation penalty (see the Figure below). However, the correlation between the total electrostatic part of the binding free energy, ++Eeleint, and the measured binding free energy is positive for both RalGDS − Ras, and Raf − Ras complexes.
Noncovalent Interactions ; proteins
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Podaci o prilogu
12-12.
2007.
objavljeno
Podaci o matičnoj publikaciji
Humboldt Conference On Noncovalent Interactions
Zarić, Snežana
Vršac: AvH
Podaci o skupu
Humboldt Conference On Noncovalent Interactions
pozvano predavanje
15.11.2007-18.11.2007
Vršac, Srbija