High-resolution NMR studies of fibrinogen-like peptides in solution: resonance assignments and conformational analysis of residues 1-23 of the A. cap alpha. chain of human fibrinogen

Journal Article · Tue Jun 14 00:00:00 EDT 1988 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00412a040· OSTI ID:6997440

Ni, F; Scheraga, H A; Lord, S T

The proton resonances of the following synthetic linear human fibrinogen-like peptides were completely assigned with two-dimensional NMR techniques in solution: Ala(1)-Asp-Ser-Gly-Glu-Gly-Asp(7)-Phe-Leu-Ala-Glu-Gly(12)-Gly(13)-Gly(14)-Val(15)-Arg(16)-Gly-Pro-Arg-Val-Val-Glu-Arg (F10), Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-Gly-Gly(13)-Gly(14)-Val-Arg (F11), and Gly-Pro-Arg-Val-Val-Glu-Arg (F12). No predominant structure was found in the chain segment from Ala(1) to Gly (6) for F10 in both H/sub 2/O and dimethyl sulfoxide. The previous suggestion that there is a hairpin loop involving residues Gly(12) to Val(15) in the A..cap alpha.. chain of human fibrinogen is supported by the slow backbone NH exchange rates of Gly(14) and Val(15), by an unusually small NH chemical shift of Val(15), and by strong sequential NOE's involving this region in F10. This local chain fold within residues Asp(7) to Val(20) may place the distant Phe residue near the Arg(16)-Gly(17) peptide bond which is cleaved by thrombin.

• Research Organization: Cornell Univ., Ithaca, NY (USA)
• OSTI ID: 6997440
• Journal Information: Biochemistry; (United States), Vol. 27:12
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
FIBRINOGEN
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
CHEMICAL SHIFT
OVERHAUSER EFFECT
PEPTIDES
BLOOD COAGULATION FACTORS
COAGULANTS
DRUGS
GLOBULINS
HEMATOLOGIC AGENTS
HEMOSTATICS
MAGNETIC RESONANCE
ORGANIC COMPOUNDS
PROTEINS
RESONANCE
550601* - Medicine- Unsealed Radionuclides in Diagnostics