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Related Concept Videos

2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene π orbitals.
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.

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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

Exploring collagen self-assembly by NMR.

Natalia Lisitza1, Xudong Huang, Hiroto Hatabu

  • 1Department of Radiology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. nlisitza@partners.org

Physical Chemistry Chemical Physics : PCCP
|September 30, 2010
PubMed
Summary
This summary is machine-generated.

The NMR signal intensity of collagen type I over time indicates protein aggregation. This aggregation is sensitive to pH and reveals insights into the underlying aggregation mechanisms.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Collagen type I is a crucial structural protein.
  • Protein aggregation is implicated in various diseases.
  • Understanding aggregation mechanisms is vital for therapeutic development.

Purpose of the Study:

  • To investigate the time-dependence of NMR signal intensity in collagen type I.
  • To correlate NMR signal changes with protein aggregation.
  • To explore the pH sensitivity of collagen aggregation.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
  • Time-resolved measurements of NMR signal intensity were performed.
  • Collagen type I solutions were studied under varying pH conditions.

Main Results:

  • NMR signal intensity decay over time reflects collagen type I aggregation.
  • The aggregation process demonstrated significant pH sensitivity.
  • Specific pH ranges correlated with distinct aggregation kinetics.

Conclusions:

  • Time-dependent NMR signal intensity is a valid indicator of collagen type I aggregation.
  • pH plays a critical role in modulating collagen aggregation.
  • NMR spectroscopy offers a valuable tool for studying protein aggregation mechanisms.