Results 241 to 250 of about 6,859,921 (298)
We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen +5 more
wiley +1 more source
Language models can identify enzymatic binding sites in protein sequences. [PDF]
Nana Teukam YG +5 more
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Improving protein function prediction by learning and integrating representations of protein sequences and function labels. [PDF]
Boadu F, Cheng J.
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iDLB-Pred: identification of disordered lipid binding residues in protein sequences using convolutional neural network. [PDF]
Malebary SJ, Alromema N.
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Co-evolution of alpha-helical transmembrane protein residues: large-scale variant profiling and complete mutational landscape of 2277 known PDB entries representing 504 unique human protein sequences. [PDF]
Karagöl T, Karagöl A, Zhang S.
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Protein complex structure modeling by cross-modal alignment between cryo-EM maps and protein sequences. [PDF]
Chen S +5 more
europepmc +1 more source
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Aligning a DNA sequence with a protein sequence
Proceedings of the first annual international conference on Computational molecular biology - RECOMB '97, 1997We develop several algorithms for the problem of aligning DNA sequence with a protein sequence. Our methods account for frameshift errors, but not for introns in the DNA sequence. Thus, they are particularly appropriate for comparing a cDNA sequence that suffers from sequencing errors with an amino acid sequence or a protein sequence database.
Zheng Zhang 0004 +2 more
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Journal of Biomolecular Structure and Dynamics, 2005
Conserved protein sequence segments are commonly believed to correspond to functional sites in the protein sequence. A novel approach is proposed to profile the changing degree of conservation along the protein sequence, by evaluating the occurrence frequencies of all short oligopeptides of the given sequence in a large proteome database.
E, Aharonovsky, E N, Trifonov
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Conserved protein sequence segments are commonly believed to correspond to functional sites in the protein sequence. A novel approach is proposed to profile the changing degree of conservation along the protein sequence, by evaluating the occurrence frequencies of all short oligopeptides of the given sequence in a large proteome database.
E, Aharonovsky, E N, Trifonov
openaire +2 more sources

