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(Yoong Ho Lim),(Mi Na Oh),(K . Hun Mok) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.8
The conformations of human insulin precursors, proinsulin and preproinsulin, are described in terms of molecular dynamics simulations. Despite the presence of the C-peptide and/or the signal peptide, molecular dynamics calculations utilizing the hydration shell model over a period of 500 ps indicate that the native conformations of the A and B chains are well conserved in both cases. These results further support the NMR spectroscopy results that the C-peptide is relatively disordered and does not influence the overall conformation of the native structure. The robustness of the native structure as demonstrated by experiment and simulation will permit future protein engineering applications, whereby the expression or purification yields can be improved upon sequence modification of the C-peptide and/or the signal peptide.
A Comparison of Three Dimensional Structures of Biosynthesized Preproinsulin and Insulin Using NMR
(Yoong Ho Lim),(Mi Na Oh),(K . Hun Mok) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.8
The solution conformation of the human insulin precursor, preproinsulin, is described in terms of NMR spectral data. NMR experiments were performed on preproinsulin, whose structure was compared with the NMR structure of native human insulin. Despite the presence of the C-peptide and/or the signal peptide, secondary structure analyses indicate that the native structures of the A and B chains are well conserved even in preproinsulin. The observed relative robustness of the native structure in precursor forms permits further protein engineering experiments where the C-peptide or N-terminal signal sequence can be altered for the purpose of increasing expression or purification yields when producing recombinant human insulin.
( Yoong Ho Lim,Yeun Joong Yong,Sung Jin Oh,Hong Keun Song ) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.4
Several flavonoid dimers were isolated and elucidated from the bark of Korean pine tree (Pinus densiflora). One of them was postulated to be a compound, epicatechin (4→7) 5,8,3`,4`-tetrahydroxy-(2R,3R)-flavan-3-ol, whose structural determination was carried out by diverse NMR techniques.
Lim, Yoong-Ho,Oh, Mi-Na,Kim, Su-Il The Korean Society for Applied Biological Chemistr 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.8
Computer aided molecular modeling can help to predict the three dimensional structure of the polypeptide without the sample. The study on soybean Bowman-Birk protease inhibitor (SBI) is valuable, because it has been recently known that SBI possesses anticarcinogenic activities and immune-stimulating properties. SBI has several isoinhibitors, whose isolation and characterization were reported in 1990. Among these, DII inhibits trypsin only. The different inhibitory specificities cannot be explained only by their different primary sequences, but is possible with further assistance by the study on their different three dimensional structures. The study on the three dimensional structure of DII using homology method is reported in this paper.
(Yoong Ho Lim),(Mi Na Oh),(Su Il Kim) 한국응용생명화학회 1998 Applied Biological Chemistry (Appl Biol Chem) Vol.41 No.8
Computer aided molecular modeling can help to predict the three dimensional structure of the polypeptide without the sample. The study on soybean Bowman-Birk protease inhibitor (SBI) is valuable, because it has been recently known that SBI possesses anticarcinogenic activities and immune-stimulating properties. SBI has several isoinhibitors, whose isolation and characterization were reported in 1990. Among these, DII inhibits trypsin only. The different inhibitory specificities cannot be explained only by their different primary sequences, but is possible with further assistance by the study on their different three dimensional structures. The study on the three dimensional structure of DII using homology method is reported in this paper.