Analysis of the differences in the folding mechanisms of c-type lysozymes based on contact maps constructed with interresidue average distances.
A method for analyzing differences in the folding mechanisms of proteins in the same family is presented. Using only information from the amino acid sequences, contact maps derived from the interresidue average distances are employed. These maps, referred to as average distance maps (ADM), are applied to the folding of c-type lysozymes. The results reveal that the ADMs of these lysozymes reflect the differences in the detailed folding mechanisms. Further possible applications of the present method are also discussed.
Nakajima
Shunsuke
S
Department of Chemistry and Bioscience, College of Industrial Technology, Kurashiki University of Science and the Arts, Kurashiki, Okayama, Japan.
Kikuchi
Takeshi
T
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D002645:Chickens; D005260:Female; D006736:Horses; D006801:Humans; D007768:Lactalbumin / Q000737:chemistry*; D008969:Molecular Sequence Data; D005810:Multigene Family; D009113:Muramidase / Q000737:chemistry* / Q000235:genetics; D010449:Peptide Mapping / Q000379:methods*; D011237:Predictive Value of Tests; D017510:Protein Folding; D017433:Protein Structure, Secondary
D000596:Amino Acids; D007768:Lactalbumin; C421864:hen egg lysozyme; D009113:Muramidase; C514728:lysozyme C, human