Mapping side chain interactions at protein helix termini

Mapping side chain interactions at protein helix termini. Newell, N. E BMC Bioinformatics, 16(1):231, July, 2015.

Interactions that involve one or more amino acid side chains near the ends of protein helices stabilize helix termini and shape the geometry of the adjacent loops, making a substantial contribution to overall protein structure. Previous work has identified key helix-terminal motifs, such as Asx/ST N-caps, the capping box, and hydrophobic and electrostatic interactions, but important questions remain, including: 1) What loop backbone geometries are favoured by each motif? 2) To what extent are multi-amino acid motifs likely to represent genuine cooperative interactions? 3) Can new motifs be identified in a large, recent dataset using the latest bioinformatics tools?

@article{newell_mapping_2015,
	title = {Mapping side chain interactions at protein helix termini},
	volume = {16},
	url = {http://www.biomedcentral.com/1471-2105/16/231},
	doi = {10.1186/s12859-015-0671-4},
	abstract = {Interactions that involve one or more amino acid side chains near the ends of protein helices stabilize helix termini and shape the geometry of the adjacent loops, making a substantial contribution to overall protein structure. Previous work has identified key helix-terminal motifs, such as Asx/ST N-caps, the capping box, and hydrophobic and electrostatic interactions, but important questions remain, including: 1) What loop backbone geometries are favoured by each motif? 2) To what extent are multi-amino acid motifs likely to represent genuine cooperative interactions? 3) Can new motifs be identified in a large, recent dataset using the latest bioinformatics tools?},
	language = {English},
	number = {1},
	journal = {BMC Bioinformatics},
	author = {Newell, Nicholas E},
	month = jul,
	year = {2015},
	pmid = {26209176},
	pmcid = {PMC4515027},
	pages = {231},
}

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