Amino acid intrinsic α-helical propensities III: Positional dependence at several positions of C terminus. Petukhov, M., Uegaki, K., Yumoto, N., & Serrano, L. Protein Science, 11(4):766-777, 2002. cited By 36![Amino acid intrinsic α-helical propensities III: Positional dependence at several positions of C terminus [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex In this study, we have analyzed experimentally the helical intrinsic propensities of noncharged and nonaromatic residues at different C-terminal positions (C1, C2, C3) of an Ala-based peptide. The effect was found to be complex, resulting in extra stabilization or destabilization, depending on guest amino acid and position under consideration. Polar (Ser, Thr, Cys, Asn, and Gln) amino acids and Gly were found to have significantly larger helical propensities at several C-terminal positions compared with the α-helix center (-1.0 kcal/mole in some cases). Some of the nonpolar residues, especially β-branched ones (Val and Ile) are significantly more favorable at position C3 (-0.3 to -0.4 kcal/mole), although having minor differences at other C-terminal positions compared with the α-helix center. Leu has moderate (-0.1 to -0.2 kcal/mole) stabilization effects at position C2 and C3, whereas being relatively neutral at C1. Finally, Met was found to be unfavorable at C1 and C2 (+0.2 kcal/mole) and favorable at C3 (-0.2 kcal/mole). Thus, significant differences found between the intrinsic helical propensities at the C-terminal positions and those in the α-helix center must be accounted for in helix/coil transition theories and in protein design.
@ARTICLE{Petukhov2002766,
author={Petukhov, M. and Uegaki, K. and Yumoto, N. and Serrano, L.},
title={Amino acid intrinsic α-helical propensities III: Positional dependence at several positions of C terminus},
journal={Protein Science},
year={2002},
volume={11},
number={4},
pages={766-777},
doi={10.1110/ps.2610102},
note={cited By 36},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036127566&doi=10.1110%2fps.2610102&partnerID=40&md5=283c9bfbf0cfe8939651d097c7bb4327},
affiliation={European Molecular Biology Laboratory (EMBL), Heidelberg, D-69012, Germany; Division of Molecular and Radiation Biology, St. Petersburg Nuclear Physics Institute, RAS, Gatchina, 188350, St. Petersburg, Russian Federation; Osaka National Research Institute, AIST, Ikeda, Osaka 563, Japan; European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, Heidelberg D-69117, Germany},
abstract={In this study, we have analyzed experimentally the helical intrinsic propensities of noncharged and nonaromatic residues at different C-terminal positions (C1, C2, C3) of an Ala-based peptide. The effect was found to be complex, resulting in extra stabilization or destabilization, depending on guest amino acid and position under consideration. Polar (Ser, Thr, Cys, Asn, and Gln) amino acids and Gly were found to have significantly larger helical propensities at several C-terminal positions compared with the α-helix center (-1.0 kcal/mole in some cases). Some of the nonpolar residues, especially β-branched ones (Val and Ile) are significantly more favorable at position C3 (-0.3 to -0.4 kcal/mole), although having minor differences at other C-terminal positions compared with the α-helix center. Leu has moderate (-0.1 to -0.2 kcal/mole) stabilization effects at position C2 and C3, whereas being relatively neutral at C1. Finally, Met was found to be unfavorable at C1 and C2 (+0.2 kcal/mole) and favorable at C3 (-0.2 kcal/mole). Thus, significant differences found between the intrinsic helical propensities at the C-terminal positions and those in the α-helix center must be accounted for in helix/coil transition theories and in protein design.},
author_keywords={α-helix; C terminus; Folding; Secondary structure},
correspondence_address1={Serrano, L.; European Molec. Biology Laboratory, Meyerhofstrasse 1, Heidelberg D-69117, Germany; email: serrano@EMBL-Heidelberg.de},
issn={09618368},
coden={PRCIE},
pubmed_id={11910021},
language={English},
abbrev_source_title={Protein Sci.},
document_type={Article},
source={Scopus},
}
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The effect was found to be complex, resulting in extra stabilization or destabilization, depending on guest amino acid and position under consideration. Polar (Ser, Thr, Cys, Asn, and Gln) amino acids and Gly were found to have significantly larger helical propensities at several C-terminal positions compared with the α-helix center (-1.0 kcal/mole in some cases). Some of the nonpolar residues, especially β-branched ones (Val and Ile) are significantly more favorable at position C3 (-0.3 to -0.4 kcal/mole), although having minor differences at other C-terminal positions compared with the α-helix center. Leu has moderate (-0.1 to -0.2 kcal/mole) stabilization effects at position C2 and C3, whereas being relatively neutral at C1. Finally, Met was found to be unfavorable at C1 and C2 (+0.2 kcal/mole) and favorable at C3 (-0.2 kcal/mole). 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