Items where Author is "Lu, Hui"
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FAD binding
Wang, Qi, Ang, Swee Kim, Ceh-Pavia, Efrain, Pang, Jiayun ORCID: 0000-0003-0689-8440 and Lu, Hui (2015) Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function. Bioscience Reports, 35 (4):e00244. ISSN 0144-8463 (Print), 1573-4935 (Online) (doi:https://doi.org/10.1042/BSR20150144)
hydrophobic effect
Ivanova, Ekaterina, Pang, Jiayun ORCID: 0000-0003-0689-8440 , Jowitt, Thomas A., Yan, Guanhua, Warwicker, Jim, Sutcliffe, Michael J. and Lu, Hui (2011) Temperature-dependent study reveals that dynamics of hydrophobic residues plays an important functional role in the mitochondrial Tim9–Tim10 complex. Proteins: Structure, Function, and Bioinformatics, 80 (2). pp. 602-615. ISSN 0887-3585 (Print), 1097-0134 (Online) (doi:https://doi.org/10.1002/prot.23224)
kinetics
Ivanova, Ekaterina, Pang, Jiayun ORCID: 0000-0003-0689-8440 , Jowitt, Thomas A., Yan, Guanhua, Warwicker, Jim, Sutcliffe, Michael J. and Lu, Hui (2011) Temperature-dependent study reveals that dynamics of hydrophobic residues plays an important functional role in the mitochondrial Tim9–Tim10 complex. Proteins: Structure, Function, and Bioinformatics, 80 (2). pp. 602-615. ISSN 0887-3585 (Print), 1097-0134 (Online) (doi:https://doi.org/10.1002/prot.23224)
mitochondria
Wang, Qi, Ang, Swee Kim, Ceh-Pavia, Efrain, Pang, Jiayun ORCID: 0000-0003-0689-8440 and Lu, Hui (2015) Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function. Bioscience Reports, 35 (4):e00244. ISSN 0144-8463 (Print), 1573-4935 (Online) (doi:https://doi.org/10.1042/BSR20150144)
protein folding
Wang, Qi, Ang, Swee Kim, Ceh-Pavia, Efrain, Pang, Jiayun ORCID: 0000-0003-0689-8440 and Lu, Hui (2015) Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function. Bioscience Reports, 35 (4):e00244. ISSN 0144-8463 (Print), 1573-4935 (Online) (doi:https://doi.org/10.1042/BSR20150144)
protein–protein interaction
Ivanova, Ekaterina, Pang, Jiayun ORCID: 0000-0003-0689-8440 , Jowitt, Thomas A., Yan, Guanhua, Warwicker, Jim, Sutcliffe, Michael J. and Lu, Hui (2011) Temperature-dependent study reveals that dynamics of hydrophobic residues plays an important functional role in the mitochondrial Tim9–Tim10 complex. Proteins: Structure, Function, and Bioinformatics, 80 (2). pp. 602-615. ISSN 0887-3585 (Print), 1097-0134 (Online) (doi:https://doi.org/10.1002/prot.23224)
simulation
Ivanova, Ekaterina, Pang, Jiayun ORCID: 0000-0003-0689-8440 , Jowitt, Thomas A., Yan, Guanhua, Warwicker, Jim, Sutcliffe, Michael J. and Lu, Hui (2011) Temperature-dependent study reveals that dynamics of hydrophobic residues plays an important functional role in the mitochondrial Tim9–Tim10 complex. Proteins: Structure, Function, and Bioinformatics, 80 (2). pp. 602-615. ISSN 0887-3585 (Print), 1097-0134 (Online) (doi:https://doi.org/10.1002/prot.23224)
stopped-flow
Ivanova, Ekaterina, Pang, Jiayun ORCID: 0000-0003-0689-8440 , Jowitt, Thomas A., Yan, Guanhua, Warwicker, Jim, Sutcliffe, Michael J. and Lu, Hui (2011) Temperature-dependent study reveals that dynamics of hydrophobic residues plays an important functional role in the mitochondrial Tim9–Tim10 complex. Proteins: Structure, Function, and Bioinformatics, 80 (2). pp. 602-615. ISSN 0887-3585 (Print), 1097-0134 (Online) (doi:https://doi.org/10.1002/prot.23224)
sulphydryl oxidase
Wang, Qi, Ang, Swee Kim, Ceh-Pavia, Efrain, Pang, Jiayun ORCID: 0000-0003-0689-8440 and Lu, Hui (2015) Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function. Bioscience Reports, 35 (4):e00244. ISSN 0144-8463 (Print), 1573-4935 (Online) (doi:https://doi.org/10.1042/BSR20150144)
tryptophan residue
Wang, Qi, Ang, Swee Kim, Ceh-Pavia, Efrain, Pang, Jiayun ORCID: 0000-0003-0689-8440 and Lu, Hui (2015) Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function. Bioscience Reports, 35 (4):e00244. ISSN 0144-8463 (Print), 1573-4935 (Online) (doi:https://doi.org/10.1042/BSR20150144)