PMC:1867812 / 23303-24329 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/1867812","sourcedb":"PMC","sourceid":"1867812","source_url":"https://www.ncbi.nlm.nih.gov/pmc/1867812","text":"As discussed in the literature [18-21], non-local patterns (where bit-patterns are one type of non-local patterns,) in contact maps can effectively capture the secondary structure of proteins. Our previous work [6,7] demonstrated that by characterizing the spatial relationship among the above described bit-patterns, one can construct structural signatures for proteins of different classes or folds. In the context of protein folding, we have observed that the above-defined bit-patterns are also capable of capturing a wide range of local 3D structural motifs. They can even approximately measure the strength of secondary structure propensity in a conformation. For instance, we have identified bit-patterns that correspond to \"premature\" α-helices and native-like α-helices respectively. Henceforth, we refer to the 3D structure formed by all the participating residues of a bit-pattern as the 3D motif of the bit-pattern. The relationship between bit-patterns and 3D motifs will be further discussed in the next section.","tracks":[{"project":"2_test","denotations":[{"id":"17407611-9806935-1692924","span":{"begin":32,"end":34},"obj":"9806935"}],"attributes":[{"subj":"17407611-9806935-1692924","pred":"source","obj":"2_test"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"2_test","color":"#ec93e5","default":true}]}]}}