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HMQC vs HSQC for Small Molecules
Kim, Eunhee,Cheong, Hae-Kap 한국자기공명학회 2017 Journal of the Korean Magnetic Resonance Society Vol.21 No.4
Proton detected Heteronuclear Multiple Quantum Coherence (HMQC) and Heteronuclear Single Quantum Coherence (HSQC) essentially provide the same information - correlation of the chemical shift of the proton to J-coupled hetero nuclei such as $^{13}C$ or $^{15}N$ nuclei. This paper is a practical note for the students who ask which one is better and which methods they use routinely. Artifact suppression using phase cycling and gradient pulses are discussed.
Crystal structure of the EnvZ periplasmic domain with CHAPS
Hwang, Eunha,Cheong, Hae-Kap,Kim, Sang-Yoon,Kwon, Ohsuk,Blain, Katherine Y.,Choe, Senyon,Yeo, Kwon Joo,Jung, Yong Woo,Jeon, Young Ho,Cheong, Chaejoon North-Holland Pub 2017 FEBS letters Vol. No.
<P>Bacteria sense and respond to osmolarity through the EnvZ-OmpR two-component system. The structure of the periplasmic sensor domain of EnvZ (EnvZ-PD) is not available yet. Here, we present the crystal structure of EnvZ-PD in the presence of CHAPS detergent. The structure of EnvZ-PD shows similar folding topology to the PDC domains of PhoQ, DcuS, and CitA, but distinct orientations of helices and beta-hairpin structures. The CD and NMR spectra of EnvZ-PD in the presence of cholate, a major component of bile salts, are similar to those with CHAPS. Chemical cross-linking shows that the dimerization of EnvZ-PD is significantly inhibited by the CHAPS and cholate. Together with beta-galactosidase assay, these results suggest that bile salts may affect the EnvZ structure and function in Escherichia coli.</P>
Lee, Chung-Kyung,Cheong, Hae-Kap,Ryu, Kyoung-Seok,Lee, Jae Il,Lee, Weontae,Jeon, Young Ho,Cheong, Chaejoon Wiley Subscription Services, Inc., A Wiley Company 2008 Proteins Vol.72 No.2
<P>Acetyl-CoA carboxylase (ACC) catalyzes the first step in fatty acid biosynthesis: the synthesis of malonyl-CoA from acetyl-CoA. As essential regulators of fatty acid biosynthesis and metabolism, ACCs are regarded as therapeutic targets for the treatment of metabolic diseases such as obesity. In ACC, the biotinoyl domain performs a critical function by transferring an activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, followed by carboxyl transfer to malonyl-CoA. Despite the intensive research on this enzyme, only the bacterial and yeast ACC structures are currently available. To explore the mechanism of ACC holoenzyme function, we determined the structure of the biotinoyl domain of human ACC2 and analyzed its characteristics and interaction with the biotin ligase, BirA using NMR spectroscopy. The 3D structure of the hACC2 biotinoyl domain has a similar folding topology to the earlier determined domains from E. coli and P. shermanii. However, the local structures near the biotinylation sites have notable differences that include the geometry of the consensus “Met-Lys-Met” (MKM) motif and the absence of “thumb” structure in the hACC2 biotinoyl domain. Observations of the NMR signals upon the biotinylation indicate that the biotin group of hACC2 does not affect the structure of the biotinoyl domain, while the biotin group for E. coli ACC interacts directly with the thumb residues that are not present in the hACC2 structure. These results imply that, in the E. coli ACC reaction, the biotin moiety carrying the carboxyl group from BC to CT can pause at the thumb of the BCCP domain. The human biotinoyl domain, however, lacks the thumb structure and does not have additional noncovalent interactions with the biotin moiety; thus, the flexible motion of the biotinylated lysine residue must underlie the “swinging arm” motion. The chemical shift perturbation and the cross saturation experiments of the human ACC2 holo-biotinoyl upon the addition of the biotin ligase (BirA) showed the interaction surface near the MKM motif, the two glutamic acids (Glu 926, Glu 953), and the positively charged residues (several lysine and arginine residues). This study provides insight into the mechanism of ACC holoenzyme function and supports the swinging arm model in human ACCs. Proteins 2008. © 2008 Wiley-Liss, Inc.</P>
윤지혜,Heeyoun Kim,박정은,Hae-kap Cheong,Chaejoon Cheong,Jung Sup Lee,이원태 대한화학회 2012 Bulletin of the Korean Chemical Society Vol.33 No.10
Vibrio extracellular metalloprotease (vEP), secreted from Vibrio vulnificus, shows various proteolytic function such as prothrombin activation and fibrinolytic activities. Premature form of vEP has an N-terminal (nPP) and a C-terminal (C-ter100) region. The nPP and C-ter100 regions are autocleaved for the matured metalloprotease activity. It has been proposed that two regions play a key role in regulating enzymatic activity of vEP. Especially, C-ter100 has a regulatory function on proteolytic activity of vEP. C-ter100 domain has been cloned into the E. coli expression vectors, pET32a and pGEX 4T-1 with TEV protease cleavage site and purified using gel-filtration chromatography followed by affinity chromatography. To understand how C-ter100 modulates proteolytic activity of vEP, structural studies were performed by heteronuclar multi-dimensional NMR spectroscopy. Backbone 1H, 15N and 13C resonances were assigned by data from standard triple resonance and HCCH-TOCSY experiments. The secondary structures of vEP C-ter100 were determined by TALOS+ and CSI software based on hydrogen/deuterium exchange. NMR data show that C-ter100 of vEP forms a β-barrel structure consisting of eight β-strands.