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Jienv Ding
National Institutes of Health
ChemistryArsenate reductaseChaperone (protein)BiochemistryBiology
4Publications
2H-index
16Citations
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Publications 6
Newest
#1Xing-Chi YuH-Index: 1
#2Yunfei HuH-Index: 12
Last. Changwen JinH-Index: 21
view all 5 authors...
1 CitationsSource
#1Xing-Chi Yu (PKU: Peking University)H-Index: 1
#2Yunfei Hu (PKU: Peking University)H-Index: 12
Last. Changwen Jin (PKU: Peking University)H-Index: 21
view all 5 authors...
The role of protein structural disorder in biological functions is gaining increasing interests in the past decade. The bacterial acid-resistant chaperone HdeA belongs to a group of 9conditionally disordered9 protein that is activated via an order-to-disorder transition. However, the mechanism for unfolding-induced activation remains unclear due to the lack of experimental information on the unfolded state conformation and the chaperone-client interactions. Here we use advanced solution NMR meth...
1 CitationsSource
#1Xiaogang Niu (PKU: Peking University)H-Index: 1
#2Jienv Ding (PKU: Peking University)H-Index: 1
Last. Changwen Jin (PKU: Peking University)H-Index: 21
view all 6 authors...
Abstract Proteins are intrinsically dynamic molecules and undergo exchanges among multiple conformations to perform biological functions. The CPMG relaxation dispersion and CEST experiments are two important solution NMR techniques for characterizing the conformational exchange processes on the millisecond timescale. Traditional pseudo 3D 15 N CEST and CPMG experiments have certain limitations in their applications. For example, both experiments have low sensitivity for broadened resonances, and...
1 CitationsSource
#1Xing-Chi YuH-Index: 1
#2Chengfeng YangH-Index: 2
Last. Changwen JinH-Index: 21
view all 6 authors...
The bacterial acid-resistant chaperone HdeA is a “conditionally disordered” protein that functions at low pH when it undergoes a transition from a well-folded dimer to an unfolded monomer. The dimer dissociation and unfolding processes result in exposure of hydrophobic surfaces that allows binding to a broad range of client proteins. To fully elucidate the chaperone mechanism of HdeA, it is crucial to understand how the activated HdeA interacts with its native substrates during acid stress. Here...
5 CitationsSource
#1Ling Guan (THU: Tsinghua University)H-Index: 1
#2Peng He (THU: Tsinghua University)H-Index: 1
Last. Daochun Kong (THU: Tsinghua University)H-Index: 13
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3 CitationsSource
#1Jienv DingH-Index: 2
#2Chengfeng YangH-Index: 2
Last. Changwen JinH-Index: 21
view all 5 authors...
Enteric bacteria encounter extreme acidity when passing through hosts’ stomach. Since the bacterial periplasmic space quickly equilibrates with outer environment, an efficient acid resistance mechanism is essential in preventing irreversible protein denaturation/aggregation and maintaining bacteria viability. HdeB, along with its homolog HdeA, was identified as a periplasmic acid-resistant chaperone. Both proteins exist as homodimers and share similar monomeric structures under neutral pH, while...
12 CitationsSource
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