CPISRTWASIFRCW CPISRTWASIFRCW Left. Same hydrophobicity and I/L about same CPISRT---LFRCW CPISRTL---FRCW size while W is much bigger. |
CPISRTRASEFRCW CPISRTRASEFRCW Left. K and R both positive and E negative. CPISRTK---FRCW CPISRT---KFRCW |
CPISRTIASNFRCW CPISRTIASNFRCW Right. H and N both hydrophilic. CPISRTH---FRCW CPISRT---HFRCW |
CPISRTEASDFRCW CPISRTEASDFRCW Left. N same size as D. Other difference is same CPISRT---NFRCW CPISRTN---FRCW between N/D and N/E plus E good for helix; N and D turn. |
CPISRTSASIFRCW CPISRTSASIFRCW Right. T and S both alcoholic and small. T/I both β-branced, CPISRT---TFRCW CPISRTT---FRCW but that is only secondary to hydrophobicity similarity. |
CPISRTGASIFRCW CPISRTGASIFRCW Now it is getting difficult. The PAM-250 matrix prefers A/G over CPISRTA---FRCW CPISRT---AFRCW A/I. In practice this will depend much on the environment. G is special because of its flexibility, but we very often find one of the three small residues (G,A,S) at the point where two helices have their cosest approach. At the Bijvoet center website I found a nice example: |
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Close helix-helix packing requires the presence of G,A,S. (In this case even 2 Gly residues). |
CPISRTEASNFRCW CPISRTEASNFRCW PAM-250 thinks this is almost the same. In practice this will CPISRTQ---FRCW CPISRT---QFRCW fully depend on the local environment in the structure. Most matrices show a preference for the left one because the one extra carbon that Q and E both have in the side chain makes them hydrophobically a bit more similar to each other than to N. |
CPISRTFASTFRCW CPISRTFASTFRCW Right. Y/F both have big aromatic ring and that is sufficiently CPISRT---YFRCW CPISRTY---FRCW much hydrophobic similarity. Also, if you like the idea of T and Y both being alcoholic then realize that if you mutate T <-> Y, you will find the alcohol group at a very different point in space. |