Prediction of the conformation of ice-nucleation protein by conformational energy calculation.
The active conformation of an ice-nucleation protein, whose major portion consists of a long polypeptide segment of nearly repetitive octapeptides, is predicted by the analyses of conformational energy and the mechanism of crystal growth. The protein ideally has an exact octapeptide repetition and is assumed to have a helical conformation. The present study searched for low-energy helical conformations and each of the obtained low-energy conformations examined as to whether it has a surface structure that can promote crystal formation. Two conformations obtained were good candidates for an ice nucleus. Both were found to have on their surfaces an arrangement of hydrogen-bonding sites, which fits well with those of hydrogen bonds in hexagonal ice crystal. Further, one of the two conformations had a hexagonal conformational symmetry consistent with the hexagonal ice crystal structure. The other conformation had a pentagonal conformational symmetry that could enable the growth of an ice crystal--dendritic polycrystalline snow crystal--which grows on metastable cubic ice.
Mizuno
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Computer Center for Medical Research, School of Medicine, Kurume University, Japan.
D000595:Amino Acid Sequence; D001483:Base Sequence; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004269:DNA, Bacterial / Q000032:analysis; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000032:analysis*; D011487:Protein Conformation; D011549:Pseudomonas / Q000032:analysis / Q000648:ultrastructure
D004269:DNA, Bacterial; D009687:Nuclear Proteins