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Internal loops helical distortion

Table II. Distortion of Helical Axes Surrounding Internal Loops... Table II. Distortion of Helical Axes Surrounding Internal Loops...
Shi et al.71 have assigned the backbone and side-chain chemical shifts for 103 of 238 residues of proteorhodopsin using solid state NMR spectroscopy. Analysis of the chemical shifts has allowed determination of protonation states of several carboxylic acids as well as boundaries and distortions of trans-membrane a-helices and secondary structure elements in the loops. It has been shown that internal Asp227, making a part of the counterion, is ionised, while Glul42 located close to the extracellular surface is neutral. [Pg.158]

See other pages where Internal loops helical distortion is mentioned: [Pg.68]    [Pg.56]    [Pg.57]    [Pg.65]    [Pg.65]    [Pg.74]    [Pg.225]    [Pg.352]   
See also in sourсe #XX -- [ Pg.65 , Pg.66 , Pg.67 ]



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Internal loops

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