Proteomics

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Intermolecular Architecture of Fibrin Clots and its Interaction INterface with Albumin


ABSTRACT: In this project we establish the unit cell of fibrin polymer network by using of XL-MS methods and modelling approaches. With shotgun proteomics approach we estimate the ratio of proteins in the purified Fibrin Clots and ratio of Albumin inter- and intralinks

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Oleg Klykov  

LAB HEAD: Albert J. R. Heck

PROVIDER: PXD011680 | Pride | 2020-01-09

REPOSITORIES: Pride

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Publications

Missing regions within the molecular architecture of human fibrin clots structurally resolved by XL-MS and integrative structural modeling.

Klykov Oleg O   van der Zwaan Carmen C   Heck Albert J R AJR   Meijer Alexander B AB   Scheltema Richard A RA  

Proceedings of the National Academy of Sciences of the United States of America 20200110 4


Upon activation, fibrinogen forms large fibrin biopolymers that coalesce into clots which assist in wound healing. Limited insights into their molecular architecture, due to the sheer size and the insoluble character of fibrin clots, have restricted our ability to develop novel treatments for clotting diseases. The, so far resolved, disparate structural details have provided insights into linear elongation; however, molecular details like the C-terminal domain of the α-chain, the heparin-binding  ...[more]

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