Feature Requests item #1588916, was opened at 2006-11-01 21:56
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Category: None
Group: None
Status: Open
Priority: 5
Private: No
Submitted By: friedar (friedar)
Assigned to: Nobody/Anonymous (nobody)
Summary: alpha carbon smooth trace/ribbon/etc.

Initial Comment:
Jmol should have an option (and actually IMO it should be the default) 
of  smooth backbone representations that follow the alpha carbon 
position rather than the current default of the peptide bond. 

Since the work to accomplish this is not trivial, I'd like to justify the 
need for this rather strongly.

There are two compelling reasons. One is that it is simply the standard 
in crystallography and NMR representations of proteins, so it is hard to 
understand why Jmol should execute this very standard representation 
differently. An alpha carbon trace has a characteristic look and feel that 
protein structure people expect to see, because it is more reflective of 
the true path of the backbone. The muted curves of the backbone in 
Jmol's sheets, turns and loops are actually quite different from the 
undulations of an alpha carbon trace/ribbon/cartoon. 

Second, in proteins there is a frequent need to display a few key side 
chains  as sticks (or ball and stick) protruding from a smooth trace or 
cartoon at an active or binding site. This type of display is used in 
almost every structure representation of a ligand binding site. With the 
current Jmol representations, the alpha carbons of these key side 
chains are hanging in space, unconnected to the backbone tracing. 
This looks odd and is, of course, incorrect. Using a strict "backbone" 
display that connects the alpha carbons with straight rods is 
insufficient, since the straight rods echo the stick nature of the 
sidechains, and it is harder for the eye to discern the side chains. The 
smooth representations are important in this context.

Thanks for listening.




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