Characterization of the nucleation step and folding of a collagen triple-helix peptide
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作者:
Xu, YJ
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Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USAUniv Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USA
Xu, YJ
[1
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Bhate, M
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Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USAUniv Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USA
Bhate, M
[1
]
Brodsky, B
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Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USAUniv Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USA
Brodsky, B
[1
]
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[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USA
Peptide T1-892 is a triple-helical peptide designed to include two distinct domains: a C-terminal (Gly-Pro-Hyp)(4) sequence, together with an N-terminal 18-residue sequence from the alpha1(I) chain of type I collagen. Folding experiments of T1-892 using CD spectroscopy were carried out at varying concentrations and temperatures, and fitting of kinetic models to the data was used to obtain information about the folding mechanism and to derive rate constants. Proposed models include a heterogeneous population of monomers with respect to cis-trans isomerization and a third-order folding reaction from competent monomer to the triple helix. Fitting results support a nucleation domain composed of all or most of the (Gly-Pro-Hyp)(4) sequence, which must be in trans form before the monomer is competent to initiate triple-helix formation. The folding of competent monomer to a triple helix is best described by an all-or-none third-order reaction. The temperature dependence of the third-order rate constant indicates a negative activation energy and provides information about the thermodynamics of the trimerization step. These CD studies complement NMR studies carried out on the same peptide at high concentrations, illustrating how the rate-limiting folding step is affected by changes in concentration. This sequence preference of repeating Gly-Pro-Hyp units for the initiation of triple-helix formation in peptide T1-892 may be related to features in the triple-helix folding of collagens.
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页码:8143 / 8151
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[21]
ENGEL J, 1991, ANNU REV BIOPHYS BIO, V20, P137, DOI 10.1146/annurev.bb.20.060191.001033
机构:Penn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USA
Ibarra-Molero, B
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Makhatadze, GI
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机构:Penn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USA
Makhatadze, GI
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Matthews, CR
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Penn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USAPenn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USA
机构:Penn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USA
Ibarra-Molero, B
;
Makhatadze, GI
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机构:Penn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USA
Makhatadze, GI
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Matthews, CR
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Penn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USAPenn State Univ, Dept Chem, Life Sci Consortium, University Pk, PA 16802 USA