Side chain contributions to the stability of alpha-helical structure in peptides

Pingchiang C. Lyu; Mark I. Liff; Luis A. Marky; Neville R. Kallenbach

doi:10.1126/science.2237416

Side chain contributions to the stability of alpha-helical structure in peptides

Pingchiang C. Lyu, Mark I. Liff, Luis A. Marky, Neville R. Kallenbach

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Short peptides that contain significant α-helical structure in aqueous solution allow the investigation of the role of amino acid side chains in stabilizing or destabilizing α-helix structure. A host-guest system of soluble synthetic peptides was designed that consisted of chains with the block sequence TyrSerGlu₄Lys₄X₃Glu ₄Lys₄, denoted EXK, in which X represents any "guest" amino acid residue. Circular dichroism spectroscopy indicates that the extent of helicity of these peptides follows the order Ala > Leu > Met > Gln > Ile > Val > Ser > Thr > Asn > Gly. This order differs from both host-guest copolymer values (Met > Ile > Leu > Ala > Gln > Val > Thr > Asn > Ser > Gly) and the tendencies of these amino acids to occur in helices in globular proteins (Ala > Met > Leu > Gln > Ile > Val > Asn, Thr > Ser > Gly), but matches the order found in a series of synthetic coiled-coil α helices, except for Ser. Proton nuclear magnetic resonance analysis of several EXK peptides indicates that these peptides are partially helical, with the helical residues favoring the amino terminus.

Original language	English (US)
Pages (from-to)	669-673
Number of pages	5
Journal	Science
Volume	250
Issue number	4981
DOIs	https://doi.org/10.1126/science.2237416
State	Published - 1990

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title = "Side chain contributions to the stability of alpha-helical structure in peptides",

abstract = "Short peptides that contain significant α-helical structure in aqueous solution allow the investigation of the role of amino acid side chains in stabilizing or destabilizing α-helix structure. A host-guest system of soluble synthetic peptides was designed that consisted of chains with the block sequence TyrSerGlu4Lys4X3Glu 4Lys4, denoted EXK, in which X represents any {"}guest{"} amino acid residue. Circular dichroism spectroscopy indicates that the extent of helicity of these peptides follows the order Ala > Leu > Met > Gln > Ile > Val > Ser > Thr > Asn > Gly. This order differs from both host-guest copolymer values (Met > Ile > Leu > Ala > Gln > Val > Thr > Asn > Ser > Gly) and the tendencies of these amino acids to occur in helices in globular proteins (Ala > Met > Leu > Gln > Ile > Val > Asn, Thr > Ser > Gly), but matches the order found in a series of synthetic coiled-coil α helices, except for Ser. Proton nuclear magnetic resonance analysis of several EXK peptides indicates that these peptides are partially helical, with the helical residues favoring the amino terminus.",

author = "Lyu, {Pingchiang C.} and Liff, {Mark I.} and Marky, {Luis A.} and Kallenbach, {Neville R.}",

year = "1990",

doi = "10.1126/science.2237416",

language = "English (US)",

volume = "250",

pages = "669--673",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

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T1 - Side chain contributions to the stability of alpha-helical structure in peptides

AU - Lyu, Pingchiang C.

AU - Liff, Mark I.

AU - Marky, Luis A.

AU - Kallenbach, Neville R.

PY - 1990

Y1 - 1990

N2 - Short peptides that contain significant α-helical structure in aqueous solution allow the investigation of the role of amino acid side chains in stabilizing or destabilizing α-helix structure. A host-guest system of soluble synthetic peptides was designed that consisted of chains with the block sequence TyrSerGlu4Lys4X3Glu 4Lys4, denoted EXK, in which X represents any "guest" amino acid residue. Circular dichroism spectroscopy indicates that the extent of helicity of these peptides follows the order Ala > Leu > Met > Gln > Ile > Val > Ser > Thr > Asn > Gly. This order differs from both host-guest copolymer values (Met > Ile > Leu > Ala > Gln > Val > Thr > Asn > Ser > Gly) and the tendencies of these amino acids to occur in helices in globular proteins (Ala > Met > Leu > Gln > Ile > Val > Asn, Thr > Ser > Gly), but matches the order found in a series of synthetic coiled-coil α helices, except for Ser. Proton nuclear magnetic resonance analysis of several EXK peptides indicates that these peptides are partially helical, with the helical residues favoring the amino terminus.

AB - Short peptides that contain significant α-helical structure in aqueous solution allow the investigation of the role of amino acid side chains in stabilizing or destabilizing α-helix structure. A host-guest system of soluble synthetic peptides was designed that consisted of chains with the block sequence TyrSerGlu4Lys4X3Glu 4Lys4, denoted EXK, in which X represents any "guest" amino acid residue. Circular dichroism spectroscopy indicates that the extent of helicity of these peptides follows the order Ala > Leu > Met > Gln > Ile > Val > Ser > Thr > Asn > Gly. This order differs from both host-guest copolymer values (Met > Ile > Leu > Ala > Gln > Val > Thr > Asn > Ser > Gly) and the tendencies of these amino acids to occur in helices in globular proteins (Ala > Met > Leu > Gln > Ile > Val > Asn, Thr > Ser > Gly), but matches the order found in a series of synthetic coiled-coil α helices, except for Ser. Proton nuclear magnetic resonance analysis of several EXK peptides indicates that these peptides are partially helical, with the helical residues favoring the amino terminus.

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