2,211 to 2,220 of 2,335 Results
JPEG Image - 1.4 MB -
MD5: 4bc884b7873e5cb9755a6efaf0bd72e6
|
JPEG Image - 1.4 MB -
MD5: c7b5a631fe078a8f099539824ac985e5
|
JPEG Image - 1.3 MB -
MD5: be55df8eec920da1007e6c58c8b7d6ab
|
JPEG Image - 1.3 MB -
MD5: 9d57119fcd7926de48711c6c69932f39
|
JPEG Image - 1.3 MB -
MD5: d48ec64d86c653fd41dde2dcb43d78d6
|
JPEG Image - 1.3 MB -
MD5: ebbc8b5040fa305a9726dd8a98a05487
|
Dec 16, 2021 - Huang Changjin
Chng, Choon Peng; Cho, Nam-Joon; Hsia, K Jimmy; Huang, Changjin, 2021, "Related data for: Role of membrane stretch in adsorption of antiviral peptides onto lipid membranes and membrane pore formation", https://doi.org/10.21979/N9/FPJXJT, DR-NTU (Data), V1, UNF:6:pmfOkZuhxM4yN0hlCtLdzw== [fileUNF]
Final research data for paper "Role of membrane stretch in adsorption of antiviral peptides onto lipid membranes and membrane pore formation" |
Dec 16, 2021 -
Related data for: Role of membrane stretch in adsorption of antiviral peptides onto lipid membranes and membrane pore formation
Unknown - 9.8 KB -
MD5: 596f9d49ae8ec74555036b2c21f6d0f5
XMGrace file containing data for AH-peptide interaction energy (averaged over lowest three energy values) vs vesicle sizes corresponding to the respective membrane area strain levels. Secondary component of Figure 4b of paper for the 0% strain data point. |
Dec 16, 2021 -
Related data for: Role of membrane stretch in adsorption of antiviral peptides onto lipid membranes and membrane pore formation
Unknown - 17.6 KB -
MD5: b68a554f6c707ce89275f30b8ce8010c
XMGrace file containing data for AH-peptide interaction energy (averaged over lowest three energy values) vs vesicle sizes corresponding to the respective membrane area strain levels. Main component of Figure 4b of paper for 5, 10, 20% strain data points. |
Dec 16, 2021 -
Related data for: Role of membrane stretch in adsorption of antiviral peptides onto lipid membranes and membrane pore formation
Tabular Data - 379 B - 7 Variables, 12 Observations - UNF:6:pmfOkZuhxM4yN0hlCtLdzw==
Excel spreadsheet containing AH peptide-membrane interaction energies for lowest-energy conformers (i.e. best membrane binders) identified from our simulations. Figure 3b of paper. |
