Related ArticlesStructural requirements for thymosin beta4 in its contact with actin. An NMR-analysis of thymosin beta4 mutants in solution and correlation with their biological activity.
Eur J Biochem. 2000 Jun;267(12):3530-8
Authors: Simenel C, Van Troys M, Vandekerckhove J, Ampe C, Delepierre M
We examined the conformational preferences of mutants of thymosin beta4, an actin monomer sequestering protein by NMR spectroscopy in 60% (v/v) trifluoroethanol. Under these conditions, the wild-type thymosin beta4 conformation consists of an alpha-helix (helix I) extending from residues 5-16 with a more stable fragment from lysine 11 to lysine 16 and a second alpha-helix (helix II) encompassing residues 31-39. The point mutations studied here are located in helix I or in the LKKTET segment (residues 17-22) that form the two main entities of interaction with the actin molecule. The alpha-1H conformational shifts allow us to investigate the helicity of the polypeptides at the residue level and to correlate these structures with their biological activity. We determine that an extension of helix I at its C-terminal end over the LKK-segment results in loss of activity. The correct termination of this helix is connected to a specific orientation of the polypeptide essential for a cooperative action of the thymosin beta4 binding entities required for full activity.
[NMR paper] Contact model for the prediction of NMR N-H order parameters in globular proteins.
Contact model for the prediction of NMR N-H order parameters in globular proteins.
Related Articles Contact model for the prediction of NMR N-H order parameters in globular proteins.
J Am Chem Soc. 2002 Oct 30;124(43):12654-5
Authors: Zhang F, Brüschweiler R
An analytical relationship is presented for the estimation of NMR S2 order parameters of N-HN vectors of the protein backbone from high-resolution protein structures. The relationship solely depends on close contacts of the peptide plane to the rest of the protein. Application of the...
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[NMR paper] TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagne
TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.
Related Articles TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.
Biochemistry. 1998 Jul 7;37(27):9650-7
Authors: Arumugam S, Hemme CL, Yoshida N, Suzuki K, Nagase H, Berjanskii M, Wu B, Van Doren SR
Surfaces of the 173 residue catalytic domain of human matrix metalloproteinase 3 (MMP-3(DeltaC)) affected by binding of the N-terminal, 126 residue inhibitory domain of human TIMP-1...
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Molecular design made to measure and the requirements - Nanotechwire.com
Molecular design made to measure and the requirements - Nanotechwire.com
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Molecular design made to measure and the requirements
Nanotechwire.com
NMR spectroscopy, a specialty of the "NMR Core Facility" at the University of Constance, provides an alternative and complementation to other methods. ...
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[NMR paper] 19F NMR study of the myosin and tropomyosin binding sites on actin.
19F NMR study of the myosin and tropomyosin binding sites on actin.
Related Articles 19F NMR study of the myosin and tropomyosin binding sites on actin.
Biochemistry. 1990 Feb 6;29(5):1348-54
Authors: Barden JA, Phillips L
Actin was labeled with pentafluorophenyl isothiocyanate at Lys-61. The label was sufficiently small not to affect the rate or extent of actin polymerization unlike the much larger fluorescein 5-isothiocyanate which completely inhibits actin polymerization . Furthermore, the label resonances in the 376.3-MHz 19F NMR spectrum...
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[NMR paper] The polyelectrolyte behavior of actin filaments: a 25Mg NMR study.
The polyelectrolyte behavior of actin filaments: a 25Mg NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The polyelectrolyte behavior of actin filaments: a 25Mg NMR study.
Biochemistry. 1999 Jun 1;38(22):7219-26
Authors: Xian W, Tang JX, Janmey PA, Braunlin WH
Under physiological conditions, filamentous actin (F-actin) is a polyanionic protein filament. Key features of the behavior of F-actin are shared with other well-characterized polyelectrolytes, in particular, duplex DNA....
Structural requirements for thymosin beta4 in its contact with actin. An NMR-analysis
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