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1H NMR sequential assignments and secondary structure analysis of human fibrinogen gamma-chain C-terminal residues

K H Mayo1, C Burke, J N Lindon

  • 1Department of Chemistry, Temple University, Philadelphia, Pennsylvania 19122.

Biochemistry
|April 3, 1990
PubMed

Insights

This study reveals the C-terminal fragment of human fibrinogen gamma-chain adopts a structured conformation, suggesting a specific role in polymerization and platelet recognition. The peptide exhibits a helix-like structure in its N-terminal region.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Chemistry

Background:

  • The human fibrinogen gamma-chain C-terminal fragment (residues 385-411) possesses critical functional domains for polymerization and platelet interaction.
  • Understanding the conformational dynamics of this fragment is key to elucidating fibrinogen's role in hemostasis.

Purpose of the Study:

  • To determine the solution conformation of the human fibrinogen gamma-chain C-terminal fragment (residues 385-411).
  • To investigate the structural basis for its biological functions in polymerization and platelet recognition.

Main Methods:

  • Isolation of the peptide fragment from cyanogen bromide degraded human fibrinogen.
  • High-field (500 MHz) proton nuclear magnetic resonance (1H NMR) spectroscopy.
  • Analysis of 2D NMR spectra (COSY, double quantum filtered COSY, HOHAHA, NOESY) for sequence-specific resonance assignments.

Main Results:

  • The N-terminal segment (residues 385-403) exhibits a relatively fixed conformation, with evidence of multiple-turn or helix-like structure (residues 390-402).
  • The C-terminal segment (residues 403-411) displays a less constrained conformation, indicated by weaker NOEs and lack of long-lived amides.
  • Significant chemical shift differences in the C-terminal dodecapeptide (residues 400-411) suggest a preferred conformation exists.

Conclusions:

  • The human fibrinogen gamma-chain C-terminal fragment possesses distinct structural features, including a helical propensity in its N-terminal portion.
  • These conformational characteristics likely underpin its dual roles in fibrinogen polymerization and platelet receptor binding.
  • The study provides insights into the structure-function relationship of a critical fibrinogen domain.

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