The time-dependence of the NMR signal intensity of collagen type I is representative of protein aggregation. It is pH sensitive and can be related to aggregation mechanism.
PMID: 20877840 [PubMed - as supplied by publisher]
Exploring translocation of proteins on DNA by NMR
Exploring translocation of proteins on DNA by NMR
Abstract While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcription factors locate their specific DNA target site within an overwhelming sea of non-specific DNA sites. Indirect kinetic data suggested that three processes are involved in the search procedure: jumping by dissociation of the protein from the DNA followed by re-association at another site,...
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08-22-2011 05:22 AM
Exploring translocation of proteins on DNA by NMR.
Exploring translocation of proteins on DNA by NMR.
Exploring translocation of proteins on DNA by NMR.
J Biomol NMR. 2011 Aug 17;
Authors: Marius Clore G
Abstract
While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcription factors locate their specific DNA target site within an overwhelming sea of non-specific DNA sites. Indirect kinetic data suggested that...
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08-19-2011 02:56 PM
Collagen atomic scale molecular disorder in ochronotic cartilage from an alkaptonuria patient, observed by solid state NMR.
Collagen atomic scale molecular disorder in ochronotic cartilage from an alkaptonuria patient, observed by solid state NMR.
Collagen atomic scale molecular disorder in ochronotic cartilage from an alkaptonuria patient, observed by solid state NMR.
J Inherit Metab Dis. 2011 Jul 7;
Authors: Chow WY, Taylor AM, Reid DG, Gallagher JA, Duer MJ
In pilot studies of the usefulness of solid state nuclear magnetic resonance spectroscopy in characterizing chemical and molecular structural effects of alkaptonuria on connective tissue, we have obtained...
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07-08-2011 05:21 PM
[NMR paper] Multiple quantum filtered NMR studies of the interaction between collagen and water i
Multiple quantum filtered NMR studies of the interaction between collagen and water in the tendon.
Related Articles Multiple quantum filtered NMR studies of the interaction between collagen and water in the tendon.
J Am Chem Soc. 2002 Mar 27;124(12):3125-32
Authors: Eliav U, Navon G
We studied the physical processes and the chemical reactions involved in magnetization transfer between water and large proteins, such as collagen, in bovine Achilles tendon. Since the NMR spectrum for such proteins is broadened by very large dipolar interactions,...
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11-24-2010 08:49 PM
[NMR paper] Effect of thermal denaturation on water-collagen interactions: NMR relaxation and dif
Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis.
Related Articles Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis.
Biopolymers. 1999 Dec;50(7):690-6
Authors: Rochdi A, Foucat L, Renou JP
The dependence of the proton spin-lattice relaxation rate, and of the enthalpy and temperature of denaturation on water content, were studied by nmr and differential scanning calorimetry (DSC) in native and...
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11-18-2010 08:31 PM
[NMR paper] NMR study of collagen-water interactions.
NMR study of collagen-water interactions.
Related Articles NMR study of collagen-water interactions.
Biopolymers. 1994 Dec;34(12):1615-26
Authors: Renou JP, Bonnet M, Bielicki G, Rochdi A, Gatellier P
A proton magnetic resonance study of different cross-linked collagens was performed as a function of water content and temperature. Collagens from three connective tissues (calf, steer, and cow) were chosen according to the different number of nonreducible multivalent cross-links, which increases during the life of animal. Samples were hydrated...
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08-22-2010 03:29 AM
[NMR paper] Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple heli
Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Related Articles Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Biochemistry. 1991 Aug 20;30(33):8251-67
Authors: Mayo KH, Parra-Diaz D, McCarthy JB,...
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08-21-2010 11:12 PM
[NMR paper] Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple heli
Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Related Articles Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state.
Biochemistry. 1991 Aug 20;30(33):8251-67
Authors: Mayo KH, Parra-Diaz D, McCarthy JB,...
Exploring collagen self-assembly by NMR.
Linear Mode
