1 to 10 of 53 Results
Feb 19, 2024
Pham, Truc Lam; Fazliev, Sunnatullo; Baur, Philipp; Comba, Peter; Thomas, Franziska, 2024, "An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnII, NiII, and CuII through a His3 Site [Research Data]", https://doi.org/10.11588/data/SIESG0, heiDATA, V1
The three-dimensional structure of a peptide, which determines its function, can denature at elevated temperatures, in the presence of chaotropic reagents, or in organic solvents. These factors limit the applicability of peptides. Herein, we present an engineered β-hairpin peptid... |
Feb 19, 2024 -
An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnII, NiII, and CuII through a His3 Site [Research Data]
ZIP Archive - 64.0 KB -
MD5: 4a81d4912263acf9f64e2a06af773cf9
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Feb 19, 2024 -
An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnII, NiII, and CuII through a His3 Site [Research Data]
ZIP Archive - 1.6 MB -
MD5: 97ffb90f626458ef1ff851991067d211
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Feb 19, 2024 -
An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnII, NiII, and CuII through a His3 Site [Research Data]
ZIP Archive - 578.3 KB -
MD5: eb5b73f4bb4c11c680a9c69ff4bbe3bf
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Feb 19, 2024 -
An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnII, NiII, and CuII through a His3 Site [Research Data]
ZIP Archive - 103.2 KB -
MD5: 57f024a5b340009a5ca6a489bb32b1ae
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Feb 19, 2024 -
An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnII, NiII, and CuII through a His3 Site [Research Data]
ZIP Archive - 34.9 KB -
MD5: 85c2c07373f70409e2ec6ea036e642ba
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Feb 19, 2024 -
An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnII, NiII, and CuII through a His3 Site [Research Data]
Adobe PDF - 242.1 KB -
MD5: 14c05ad5d29eb1144900e46db3cfd3b3
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Feb 9, 2024
Pham, Truc Lam; Conde González, Marcos Rafael; Fazliev, Sunnatullo; Kishore, Agi; Comba, Peter; Thomas, Franziska, 2024, "Relationship of Thermostability and Binding Affinity in Metal-binding WW-Domain Minireceptors [Research Data]", https://doi.org/10.11588/data/QSJTR0, heiDATA, V1
The design of metallo-miniproteins advances our understanding of the structural and functional roles of metals in proteins. We recently designed a metal-binding WW domain, WW-CA-Nle, which displays three histidine residues on its surface for coordination of divalent metals Ni(II)... |
Feb 9, 2024 -
Relationship of Thermostability and Binding Affinity in Metal-binding WW-Domain Minireceptors [Research Data]
ZIP Archive - 97.0 KB -
MD5: ab10c9a54d048229b38379f95777d139
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Feb 9, 2024 -
Relationship of Thermostability and Binding Affinity in Metal-binding WW-Domain Minireceptors [Research Data]
ZIP Archive - 3.4 MB -
MD5: ed32d600047a74b7e5615f3aa90089ed
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