Hello,

van der Waals interactions are very weak, this is why we usually speak about 
van der Waals contacts rather than interactions.
These are usually in the range of 3.5-3.8/4 Å (smaller than that may indicate a 
close contact or steric clash of an atomic model under refinement), 
corresponding to the packing of the van der Waals spheres of the individual 
atoms.
In hydrogen bond interactions, the term “interaction” normally implies sharing 
a hydrogen atom between two polar residues, for example between the hydroxyl 
group of a threonine side chain with a carbonyl group of the main chain peptide 
backbone; in there one should take into account the geometry as well (e.g. 
~120°-180° is favorable, 90° is not). Note that some positions such as Calpha-H 
can be slightly polarized (these contribute to bifurcated H-bonds in beta 
sheets for example, see e.g. https://www.ncbi.nlm.nih.gov/pubmed/12220491 ).
In the context of series of van der Waals contacts between hydrophobic residues 
there can be additive effects of the weak interactions with then sum up, but in 
this context one should also consider entropic effects such as de-solvatation 
which becomes favorable energetically.

Hope this helps.

Best regards,

Bruno


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Bruno P. Klaholz
Centre for Integrative Biology
Institute of Genetics and of Molecular and Cellular Biology
67404 ILLKIRCH
FRANCE
http://igbmc.fr/Klaholz




From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of chemocev 
marker
Sent: 08 December 2017 07:55
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Van der waals force

Hi
I just have a basic question if the Van der waals interaction will exist 
between the hydrophobic residues or it can also be contributed by the polar 
residues as well. What distance is required for the Van der waals interaction.
best
Jiri

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