pdb files (Multispan)
90
Structured Review
Multispan
pdb files
![The experimentally tested sequences are embedded as large points with black outlines. ( A ) UMAP embeddings with UniProt-derived sequences colored light blue if found in soluble domains and beige if found in TM domains. The UMAP embeddings cluster into two large lobes, delineating helices within soluble proteins from TM helices. All sequences tested with the LepB glycosylation assay (table S2) were visually clustered based on their embeddings and the predicted statistics over the three dispositions [aqueous ( P Wat <t>),</t> <t>interfacial</t> ( P Int ), and TM ( P TM )] are shown as histograms. Each of the three helical dispositions rapidly becomes more dominant along a particular direction in the UMAP space, shown by the three vectors using the same color scheme for the three dispositions as in (green, yellow, and red for inserted, interfacial, and translocated location, respectively). ( B ) The same UMAP embeddings, colored according to average hydrophobicity computed using the Δ G <t>PDB</t> scale, show a clear trend toward higher hydrophobicity (i.e., lower average Δ G PDB ) for helices from soluble proteins from left to right. ( C ) UMAP embeddings of helical peptides with known function appear in distinct regions of the UMAP space. AMPs, which tend to be soluble and negatively charged, cluster in the upper half of the left lobe. Lytic peptides and the C-terminal segments of viral fusion proteins occupy the boundary region where helices from soluble proteins and TM proteins can be found. TM viral fusion domains, which must insert into a TM state to function, can be found at the rightmost edge of the right lobe, implying a strong preference for the TM disposition. Points labeled with circular markers represent individual sequences, while diamonds represent means in the UMAP space over a functional family.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_7994/pmc11837994/pmc11837994__sciadv.ads6804-f5.jpg)
Pdb Files, supplied by Multispan, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pdb files/product/Multispan
Average 90 stars, based on 1 article reviews
Pdb Files, supplied by Multispan, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pdb files/product/Multispan
Average 90 stars, based on 1 article reviews
pdb files - by Bioz Stars,
2026-03
90/100 stars
Images
1) Product Images from "Sequence-dependent scale for translocon-mediated insertion of interfacial helices in membranes"
Article Title: Sequence-dependent scale for translocon-mediated insertion of interfacial helices in membranes
Journal: Science Advances
doi: 10.1126/sciadv.ads6804
Figure Legend Snippet: The experimentally tested sequences are embedded as large points with black outlines. ( A ) UMAP embeddings with UniProt-derived sequences colored light blue if found in soluble domains and beige if found in TM domains. The UMAP embeddings cluster into two large lobes, delineating helices within soluble proteins from TM helices. All sequences tested with the LepB glycosylation assay (table S2) were visually clustered based on their embeddings and the predicted statistics over the three dispositions [aqueous ( P Wat ), interfacial ( P Int ), and TM ( P TM )] are shown as histograms. Each of the three helical dispositions rapidly becomes more dominant along a particular direction in the UMAP space, shown by the three vectors using the same color scheme for the three dispositions as in (green, yellow, and red for inserted, interfacial, and translocated location, respectively). ( B ) The same UMAP embeddings, colored according to average hydrophobicity computed using the Δ G PDB scale, show a clear trend toward higher hydrophobicity (i.e., lower average Δ G PDB ) for helices from soluble proteins from left to right. ( C ) UMAP embeddings of helical peptides with known function appear in distinct regions of the UMAP space. AMPs, which tend to be soluble and negatively charged, cluster in the upper half of the left lobe. Lytic peptides and the C-terminal segments of viral fusion proteins occupy the boundary region where helices from soluble proteins and TM proteins can be found. TM viral fusion domains, which must insert into a TM state to function, can be found at the rightmost edge of the right lobe, implying a strong preference for the TM disposition. Points labeled with circular markers represent individual sequences, while diamonds represent means in the UMAP space over a functional family.
Techniques Used: Derivative Assay, Glycoproteomics, Labeling, Functional Assay