Model peptide studies of sequence repeats derived from the intracrystalline biomineralization protein, SM50. I. GVGGR and GMGGQ repeats

Guangzhao Xu, John Evans

Research output: Contribution to journalArticle

Abstract

We report solution-state pulsed field gradient nmr studies of a native sequence-derived 23-residue peptidomimetic, N(α)-acetyl- QPGVGGRQPGMGGQPGVGGRQPG-C(α)-amide, that incorporates the prevalent GVGGR and GMGGQ repeats found in the sea urchin embryo intracrystalline spicule matrix protein, SM50 (Strongylocentrotus purpuratus). These repeats are sequence homologues of elastin protein repeats (VPGVG, VGGVG, and APGVGV) and spider dragline silk protein repeats (GPGG, GQGG, and QPGYG). Using rotating frame nuclear Overhauser effect (ROE) connectivities, CH(α) proton conformational shifts, 3J(NH-CHα) coupling constants, amide temperature shift coefficients, and pulsed field gradient ROE spectroscopy solvent exchange measurements, we find that the 23-mer peptidomimetic possesses a multiple β-turn structure in aqueous solution, in equilibria with an extended or coil structure (60% β-turn: 40% random coil). The GVGGR sequence adopts a double β-turn conformation that is stabilized by two hydrogen bonds (R7→V4, R20→V17; G6→G3, G19→G16). The GMGGQ region adopts a single β- turn conformation that is stabilized by a hydrogen bond involving residues Q14 and M11. Repeating β-turn structures, or β-spirals, may play an important role with regard to matrix assembly, protein stability, molecular elasticity, and/or protein-crystal recognition within the spicule mineralized matrix.

Original languageEnglish (US)
Pages (from-to)303-312
Number of pages10
JournalBiopolymers - Peptide Science Section
Volume49
Issue number4
DOIs
StatePublished - Apr 5 1999

Fingerprint

Peptidomimetics
Biomineralization
valyl-prolyl-glycyl-valyl-glycine
Amides
Peptides
Hydrogen
Strongylocentrotus purpuratus
Proteins
Amino Acid Sequence Homology
Sea Urchins
Elastin
Protein Stability
Elasticity
Conformations
Protons
Spectrum Analysis
Hydrogen bonds
Embryonic Structures
Temperature
Silk

Keywords

  • Biomineralization
  • Elastin
  • Matrix proteins
  • nmr
  • Pulsed-field gradient
  • Sea urchin embryo
  • Sea urchin spicule
  • Spider silk dragline
  • β-turn

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics

Cite this

@article{a27ade809a38441985925f0ba8f922e1,
title = "Model peptide studies of sequence repeats derived from the intracrystalline biomineralization protein, SM50. I. GVGGR and GMGGQ repeats",
abstract = "We report solution-state pulsed field gradient nmr studies of a native sequence-derived 23-residue peptidomimetic, N(α)-acetyl- QPGVGGRQPGMGGQPGVGGRQPG-C(α)-amide, that incorporates the prevalent GVGGR and GMGGQ repeats found in the sea urchin embryo intracrystalline spicule matrix protein, SM50 (Strongylocentrotus purpuratus). These repeats are sequence homologues of elastin protein repeats (VPGVG, VGGVG, and APGVGV) and spider dragline silk protein repeats (GPGG, GQGG, and QPGYG). Using rotating frame nuclear Overhauser effect (ROE) connectivities, CH(α) proton conformational shifts, 3J(NH-CHα) coupling constants, amide temperature shift coefficients, and pulsed field gradient ROE spectroscopy solvent exchange measurements, we find that the 23-mer peptidomimetic possesses a multiple β-turn structure in aqueous solution, in equilibria with an extended or coil structure (60{\%} β-turn: 40{\%} random coil). The GVGGR sequence adopts a double β-turn conformation that is stabilized by two hydrogen bonds (R7→V4, R20→V17; G6→G3, G19→G16). The GMGGQ region adopts a single β- turn conformation that is stabilized by a hydrogen bond involving residues Q14 and M11. Repeating β-turn structures, or β-spirals, may play an important role with regard to matrix assembly, protein stability, molecular elasticity, and/or protein-crystal recognition within the spicule mineralized matrix.",
keywords = "Biomineralization, Elastin, Matrix proteins, nmr, Pulsed-field gradient, Sea urchin embryo, Sea urchin spicule, Spider silk dragline, β-turn",
author = "Guangzhao Xu and John Evans",
year = "1999",
month = "4",
day = "5",
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language = "English (US)",
volume = "49",
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T1 - Model peptide studies of sequence repeats derived from the intracrystalline biomineralization protein, SM50. I. GVGGR and GMGGQ repeats

AU - Xu, Guangzhao

AU - Evans, John

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N2 - We report solution-state pulsed field gradient nmr studies of a native sequence-derived 23-residue peptidomimetic, N(α)-acetyl- QPGVGGRQPGMGGQPGVGGRQPG-C(α)-amide, that incorporates the prevalent GVGGR and GMGGQ repeats found in the sea urchin embryo intracrystalline spicule matrix protein, SM50 (Strongylocentrotus purpuratus). These repeats are sequence homologues of elastin protein repeats (VPGVG, VGGVG, and APGVGV) and spider dragline silk protein repeats (GPGG, GQGG, and QPGYG). Using rotating frame nuclear Overhauser effect (ROE) connectivities, CH(α) proton conformational shifts, 3J(NH-CHα) coupling constants, amide temperature shift coefficients, and pulsed field gradient ROE spectroscopy solvent exchange measurements, we find that the 23-mer peptidomimetic possesses a multiple β-turn structure in aqueous solution, in equilibria with an extended or coil structure (60% β-turn: 40% random coil). The GVGGR sequence adopts a double β-turn conformation that is stabilized by two hydrogen bonds (R7→V4, R20→V17; G6→G3, G19→G16). The GMGGQ region adopts a single β- turn conformation that is stabilized by a hydrogen bond involving residues Q14 and M11. Repeating β-turn structures, or β-spirals, may play an important role with regard to matrix assembly, protein stability, molecular elasticity, and/or protein-crystal recognition within the spicule mineralized matrix.

AB - We report solution-state pulsed field gradient nmr studies of a native sequence-derived 23-residue peptidomimetic, N(α)-acetyl- QPGVGGRQPGMGGQPGVGGRQPG-C(α)-amide, that incorporates the prevalent GVGGR and GMGGQ repeats found in the sea urchin embryo intracrystalline spicule matrix protein, SM50 (Strongylocentrotus purpuratus). These repeats are sequence homologues of elastin protein repeats (VPGVG, VGGVG, and APGVGV) and spider dragline silk protein repeats (GPGG, GQGG, and QPGYG). Using rotating frame nuclear Overhauser effect (ROE) connectivities, CH(α) proton conformational shifts, 3J(NH-CHα) coupling constants, amide temperature shift coefficients, and pulsed field gradient ROE spectroscopy solvent exchange measurements, we find that the 23-mer peptidomimetic possesses a multiple β-turn structure in aqueous solution, in equilibria with an extended or coil structure (60% β-turn: 40% random coil). The GVGGR sequence adopts a double β-turn conformation that is stabilized by two hydrogen bonds (R7→V4, R20→V17; G6→G3, G19→G16). The GMGGQ region adopts a single β- turn conformation that is stabilized by a hydrogen bond involving residues Q14 and M11. Repeating β-turn structures, or β-spirals, may play an important role with regard to matrix assembly, protein stability, molecular elasticity, and/or protein-crystal recognition within the spicule mineralized matrix.

KW - Biomineralization

KW - Elastin

KW - Matrix proteins

KW - nmr

KW - Pulsed-field gradient

KW - Sea urchin embryo

KW - Sea urchin spicule

KW - Spider silk dragline

KW - β-turn

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U2 - 10.1002/(SICI)1097-0282(19990405)49:4<303::AID-BIP5>3.0.CO;2-4

DO - 10.1002/(SICI)1097-0282(19990405)49:4<303::AID-BIP5>3.0.CO;2-4

M3 - Article

VL - 49

SP - 303

EP - 312

JO - Biopolymers

JF - Biopolymers

SN - 0006-3525

IS - 4

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