Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM.

Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM. Abstract Text:

Brown,Rustem I Litvinov,Dennis E Discher,John W Weisel, Brown,Rustem I Litvinov,Dennis E Discher,John W Weisel,

Fibrinogen is a blood plasma protein that, after activation by thrombin, assembles into fibrin fibers that form the elastic network of blood clots. We used atomic force microscopy to study the forced unfolding of engineered linear oligomers of fibrinogen, and we show that forced extension of the oligomers produces sawtooth patterns with a peak-to-peak length consistent with the independent unfolding of the coiled-coils in a cooperative two-state manner. In contrast with force plateaus seen for myosin coiled-coils that suggested rapid refolding of myosin, Monte Carlo simulations of fibrinogen unfolding confirm that fibrinogen refolding is negligible on experimental timescales. The distinct behavior of fibrinogen seems to be due to its topologically complex coiled-coils and an interaction between fibrinogen's alphaC-domains and its central region.

Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM. Publishing Authors By Initials

AE Brown,RI Litvinov,DE Discher,JW Weisel,AE Brown,RI Litvinov,DE Discher,JW Weisel,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biophysical journal

VOLUME: 92

Page Numbers: L39-41

Journal Abbreviation: Biophys. J.

ISSN: 0006-3495

DAY: 15

MONTH: 12

YEAR: 2006

Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370626

Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM.

AFFILIATION: Department of Physics and Astronomy, Nano/Bio Interface Center, University of Pennsylvania, Philadelphia, Pennsylvania.

Country: United States

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: Biophys J

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM Related Publications

• Biophysics. Enigmas of blood clot elasticity.
• Calcium channel blockers in myocardial and cerebral ischemia: a clinician's review from bench to bedside.
• Cell transplantation: back to the bench: introduction.
• Choroidal detachment in the surgical treatment of retinal separation.
• Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.
• Dynamic imaging of fibrin network formation correlated with other measures of polymerization.
• Fibrinogen Guarenas, an abnormal fibrinogen with an Aalpha-chain truncation due to a nonsense mutation at Aalpha 467 Glu (GAA)-->stop (TAA).
• Forced Unfolding of Coiled-Coils in Fibrinogen by Single-Molecule AFM.
• Future directions of vitamin E and its analogues in minimizing myocardial ischemia-reperfusion injury.
• Glycaemic control improves fibrin network characteristics in type 2 diabetes - A purified fibrinogen model.
• Haemostatic changes related to fibrin formation and fibrinolysis during the first trimester in normal pregnancy and in recurrent miscarriage.
• Homophenotypic Aalpha R16H fibrinogen (Kingsport): uniquely altered polymerization associated with slower fibrinopeptide A than fibrinopeptide B release.
• Interactions mediated by the N-terminus of fibrinogen's Bbeta chain.
• Passive dosimeters for nitrogen dioxide in personal/indoor air sampling: a review.
• Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions.
• Relation of salinity to the activity of the spermatozoa of Gillichthys, a marine teleost.
• Sodium-Hydrogen Exchange Inhibition by Cariporide to Reduce the Risk of Ischemic Cardiac Events in Patients Undergoing Coronary Artery Bypass Grafting: Results of the EXPEDITION Study.
• Structure of fibrin: impact on clot stability.
• Which knobs fit into which holes in fibrin polymerization?