MacArthur, MW and Thornton, JM (1999) Protein side-chain conformation: a systematic variation of chi 1 mean values with resolut. Acta Crystallographica Section D , 55 (5) 994 - 1004.
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A systematic variation with resolution of the mean values of the gauche- , trans and gauche+ chi1 rotamers in protein structures determined by X- ray crystallography has been observed. Further analysis revealed that these correlations differ considerably between residue types, being highly significant for some residue types (e.g. Ser, Thr, Leu, Lys) and absent for others (e.g. aromatics). For the individual residue types which exhibited the trend most strongly, these changes were accompanied by corresponding systematic variations in the percentage relative populations in the three energy wells. Examination of a uniformly sized subset of monomers showed that this effect, while attenuated, was still present, and was thus not entirely a consequence of the change in size and surface area which also correlates with resolution. An analysis of B values in the disfavoured high-energy barrier region between the rotameric wells showed a pronounced tendency towards larger than average values. As a plausible hypothesis, it is suggested here that these observations can be accounted for by the presence of multiple rotameric states. The averaged electron density produced by dual occupancy at low resolution giving an averaged conformation is resolved at high resolution into its individual components
|Title:||Protein side-chain conformation: a systematic variation of chi 1 mean values with resolut|
|Additional information:||UI - 99234351 LA - Eng RN - 0 (Proteins) RN - 0 (Solvents) RN -52-90-4 (Cysteine) RN - 56-84-8 (Aspartic Acid) RN - 7006-34-0 (Asparagine) PT - JOURNAL ARTICLE DA - 19990630 IS - 0907-4449 SB - M CY - DENMARK JC - C3C AA - Author EM - 199909|
|Keywords:||Proteins, Solvents, Cysteine, Aspartic Acid, Acids, analysis, Asparagine, Biochemistry, chemistry, Comparative Study, Crystallography, X-Ray, Methods, modelling, Molecular Biology, Protein Conformation, Protein Structure, Rotation, Solubility, Support, Non-U.S.Gov't, Structure, Ly, ANS|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)|
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