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The rhombohedral crystal structure of [Trp]~(B1)-insulin has been refined, using data to 2 and atomic coordinates of 2-zinc porcine insulin as starting model, and through the use of the restrained least-squares method, to an R value of 0.24. The result of refinement shows that in comparison with the 2-zinc insulin structure, some changes in local conformation occur, and are asymmetric for the two independent molecules related by a local two-fold axis. The obvious conformational changes are found to be in molecule 1, at its B-chain N-terminus and A13-residue region.
The rhombohedral crystal structure of [Trp] ~ (B1) -insulin has been refined, using data to 2 and atomic coordinates of 2-zinc porcine insulin as starting model, and through the use of the restrained least-squares method, to an R value of 0.24. The result of refinement shows that in comparison with the 2-zinc insulin structure, some changes in local conformation occur, and are asymmetric for the two independent molecules related by a local two-fold axis. The obvious conformational changes are found to be in molecule 1, at its B-chain N-terminus and A13-residue region.