TITLE

Micro- and mesoscopic process interactions in protein coagulation

AUTHOR(S)
San Biagio, P. L.; Martorana, V.; Emanuele, A.; Vaiana, S. M.; Manno, M.; Bulone, D.; Palma-Vittorelli, M. B.; Palma, M. U.
PUB. DATE
April 2000
SOURCE
AIP Conference Proceedings;2000, Vol. 513 Issue 1, p214
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
It has recently been recognized that pathological protein coagulation is responsible for lethal pathologies as diverse as amyloidosis, Alzheimer and TSE. Understanding the coagulation mechanisms is therefore stirring great interest. In previous studies we have shown that on profoundly different systems coagulation is the result of a strong interaction between two processes on different length scales (mesoscopic and microscopic). Here we report experiments on bovine serum albumin (BSA) showing that the overall mechanism is the result of at least 3 distinct and strongly intertwined processes, on both length scales: molecular conformational changes, solution demixing and intermolecular crosslinking. This mechanism involves the statistical mechanics of protein-solvent interaction, its relation to the protein’s landscape of configurational free energy and to the solution’s thermodynamic stability, and its relation to the topological problem of crosslink-percolation, responsible for coagulation. © 2000 American Institute of Physics.
ACCESSION #
6028449

 

Related Articles

  • Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers. Feld, Geoffrey K.; Thoren, Katie L.; Kintzer, Alexander F.; Sterling, Harry J.; Tang, Iok I.; Greenberg, Shoshana G.; Williams, Evan R.; Krantz, Bryan A. // Nature Structural & Molecular Biology;Nov2010, Vol. 17 Issue 11, p1383 

    The protein transporter anthrax lethal toxin is composed of protective antigen (PA), a transmembrane translocase, and lethal factor (LF), a cytotoxic enzyme. After its assembly into holotoxin complexes, PA forms an oligomeric channel that unfolds LF and translocates it into the host cell. We...

  • Binding of Ca and Zn to factor IX/X-binding protein from venom of Agkistrodon halys Pallas: stabilization of the structure during GdnHCl-induced and thermally induced denaturation. Wu, Hao; Xu, Xiaolong; Shen, Dengke; Peng, Lili; Song, Jiajia; Zhang, Yan // Journal of Biological Inorganic Chemistry;Jan2011, Vol. 16 Issue 1, p69 

    Coagulation factor IX/coagulation factor X binding protein from the venom of Agkistrodon halys Pallas (AHP IX/X-bp) is a unique coagulation factor IX/coagulation factor X binding protein (IX/X-bp). Among all IX/X-bps identified, only AHP IX/X-bp is a Ca- and Zn-binding protein. The binding...

  • Engineering fluorescent protein substrates for the AAA+ Lon protease. Wohlever, Matthew L.; Nager, Andrew R.; Baker, Tania A.; Sauer, Robert T. // PEDS: Protein Engineering, Design & Selection;Apr2013, Vol. 26 Issue 4, p299 

    AAA+ proteases, such as Escherichia coli Lon, recognize protein substrates by binding to specific peptide degrons and then unfold and translocate the protein into an internal degradation chamber for proteolysis. For some AAA+ proteases, attaching specific degrons to the N- or C-terminus of green...

  • Kinetic theory of amyloid fibril templating. Schmit, Jeremy D. // Journal of Chemical Physics;May2013, Vol. 138 Issue 18, p185102 

    The growth of amyloid fibrils requires a disordered or partially unfolded protein to bind to the fibril and adapt the same conformation and alignment established by the fibril template. Since the H-bonds stabilizing the fibril are interchangeable, it is inevitable that H-bonds form between...

  • Engineering of a femtomolar affinity binding protein to human serum albumin. Andreas Jonsson; Jakob Dogan; Nina Herne; Lars Abrahmsén; Per-Åke Nygren // PEDS: Protein Engineering, Design & Selection;Aug2008, Vol. 21 Issue 8, p515 

    We describe the development of a novel serum albumin binding protein showing an extremely high affinity (KD) for HSA in the femtomolar range. Using a naturally occurring 46-residue three-helix bundle albumin binding domain (ABD) of nanomolar affinity for HSA as template, 15 residues were...

  • Mechanical unfolding of proteins L and G with constant force: Similarities and differences. Glyakina, A. V.; Balabaev, N. K.; Galzitskaya, O. V. // Journal of Chemical Physics;7/28/2009, Vol. 131 Issue 4, p045102 

    Mechanical unfolding of proteins L and G, which have similar structures, is considered in this work, and the question arises what changes happen in the unfolding pathways under the action of mechanical force. Molecular dynamics simulations with explicit water (134 trajectories) demonstrate that...

  • Ca and Mg binding induce conformational stability of Calfumirin-1 from Dictyostelium discoideum. MALLICK, BAIRAGI; KANG, SA-OUK; JHA, SUMAN // Journal of Chemical Sciences;May2014, Vol. 126 Issue 3, p751 

    The apo-Calfumirin-1 (CAF-1) binds to Ca with high affinity and also to Mg with high positive cooperativity. The thermal unfolding curves of wtCAF-1 monitored at neutral pH by CD spectroscopy are reversible and show different thermal stabilities in the absence or presence of Ca and Mg ions....

  • Understanding Pre-Structured Motifs (PreSMos) in Intrinsically Unfolded Proteins. Si-Hyung Lee; Do-Hyoung Kim; Han, Joan J.; Eun-Ji Cha; Ji-Eun Lim; Ye-Jin Cho; Chewook Lee; Kyou-Hoon Han // Current Protein & Peptide Science;Feb2012, Vol. 13 Issue 1, p34 

    Intrinsically unfolded proteins (IUPs) do not obey the golden rule of structural biology, 3D structure = function, as they manifest their inherent functions without resorting to three-dimensional structures. Absence of a compact globular topology in these proteins strongly implies that their...

  • The cohesin ring concatenates sister DNA molecules. Haering, Christian H.; Farcas, Ana-Maria; Arumugam, Prakash; Metson, Jean; Nasmyth, Kim // Nature;7/17/2008, Vol. 454 Issue 7202, p297 

    Sister chromatid cohesion, which is essential for mitosis, is mediated by a multi-subunit protein complex called cohesin. Cohesin’s Scc1, Smc1 and Smc3 subunits form a tripartite ring structure, and it has been proposed that cohesin holds sister DNA molecules together by trapping them...

Share

Read the Article

Courtesy of VIRGINIA BEACH PUBLIC LIBRARY AND SYSTEM

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics