http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Chlamydia psittaci strain fransis의 plasmid pCpA1과 C. psittaci strain 6BC의 plasmid의 염기서열 상동성 분석
한상훈,정규회,G. V. Stokes,윤병수 경기대학교 1999 論文集 Vol.43 No.2
In Chlamydia, there is not efficient transformation vector system. This defect makes hard to study of Chlamydia. As a first process for E. coli-to-chlamydia shuttle vector construction, we executed DNA sequencing analysis of Chlamydia psittaci 6BC plasmid whole origine and parts of ORFs. We compared them with already known Chlamydia psittaci francis pCpA1 whole origine and parts of ORFs sequences using Computer DNA sequence analysis program PCGENE and demonstrated that partially analyzed origins and ORFs on two plasmids matched perfectly each other.
Kyou Hoon Han,Cheorl Ho Kim,Dong Ho Choung,Kyu Hwan Park,Dae Sil Lee 생화학분자생물학회 1993 BMB Reports Vol.26 No.5
In order to determine the composition of a tetrasaccharide obtained from glycosylated barley β-amylase isozyme we applied two-dimensional (2-D) nmr (nuclear magnetic resonance) techniques. COSY (COrrelated SpectroscopY) and TOCSY (TOtally Correlated SpectroscopY) pulse sequences enabled us to achieve an unambiguous assignment of four monosaccharide units by allowing us to follow the shift-correlation map in each monomeric ring. After careful comparison to proton chemical shifts as well as the resonance patterns in literature we have found that there are α-D-G1cNAc, β-D-G1cNAc, α-D-Man and β-D-Man in the tetrasaccharide.
Kyou Hoon Han,Seung Moak Kim,Dong Ho Choung,Kyu Hwan Park,Tae Sung Moon,Dong Yeon Chae,Soo Kyung Kim,Hyun Jun Yoo 생화학분자생물학회 1994 BMB Reports Vol.27 No.4
A combination of the nuclear magnetic resonance (NMR) technique and the molecular modelling method has been successfully applied to determine high resolution solution conformations of a 17-residue oligopeptide LQARILAVERYLKDQQL (583-599) of gp41 from human immunodeficiency virus type I (HIV1), and its mutant with Ala→Thr at position 589. Vamous two-dimensional NMR methods such as NOESY (two-dimensional NOE SpectroscopY), ROESY (two-dimensional Rotating-frame nOE SpectroscopY), TOCSY (TOtal shift Correlation Spectroscopy), and COSY (shift Correlation Spectroscopy) have been used to obtain complete H-1 resonance assignments. Interproton distances obtained from NOE were input for a subsequent restrained molecular dynamics simulation. The overall shapes of both peptides are a-helical, except at the N- and C-termini. The threonyl side chain at position 589 in the mutant peptide protrudes outwards from the helical axis more than the alanyl side chain at the same position, which might account for differences in the antibody recognition patterns for the two peptides.
Han, Kyou-Hoon,Kim, Cheorl-Ho,Choung, Dong-Ho,Park, Kyu-Hwan,Lee, Dae-Sil 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.5
In order to determine the composition of a tetrasaccharide obtained from glycosylated barley ${\beta}-Amylase$ isozyme we applied two-dimensional (2-D) nmr (nuclear magnetic resonance) techniques. COSY (COrrelated SpectroscopY) and TOCSY (TOtally Correlated SpectroscopY) pulse sequences enabled us to achieve an unambiguous assignment of four monosaccharide units by allowing us to follow the shift-correlation map in each monomeric ring. After careful comparison to proton chemical shifts as well as the resonance patterns in literature we have found that there are ${\alpha}-D-GlcNAc$, ${\beta}-D-GlcNAc$, ${\alpha}-D-Man$ and ${\beta}-D-Man$ in the tetrasaccharide.
Han, Kyou-Hoon,Kim, Seung-Moak,Choung, Dong-Ho,Park, Kyu-Hwan,Moon, Tae-Sung,Chae, Dong-Yeon,Kim, Soo-Kyung,Yoo, Hyun-Ju 생화학분자생물학회 1994 한국생화학회지 Vol.27 No.4
A combination of the nuclear magnetic resonance (NMR) technique and the molecular modelling method has been successfully applied to determine high resolution solution conformations of a 17-residue oligopeptide LQARILAVERYLKDQQL (583-599) of gp41 from human immunodeficiency virus type I (HIV-1), and its mutant with Ala${\rightarrow}$Thr at position 589. Various two-dimensional NMR methods such as NOESY (two-dimensional NOE SpectroscopY), ROESY (two-dimensional Rotating-frame nOE SpectroscopY), TOCSY (TOtal shift Correlation SpectroscopY), and COSY (shift COrrelation SpectroscopY) have been used to obtain complete H-1 resonance assignments. Interproton distances obtained from NOE were input for a subsequent restrained molecular dynamics simulation. The overall shapes of both peptides are ${\alpha}$-helical, except at the N- and C-termini. The threonyl side chain at position 589 in the mutant peptide protrudes outwards from the helical axis more than the alanyl side chain at the same position, which might account for differences in the antibody recognition patterns for the two peptides.