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Structures of Solids02:22

Structures of Solids

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Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
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NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

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In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
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Structural Protein Function01:56

Structural Protein Function

30.0K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
30.0K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.4K
Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
6.4K
NMR Spectroscopy of Benzene Derivatives01:34

NMR Spectroscopy of Benzene Derivatives

11.3K
Simple unsubstituted benzene has six aromatic protons, all chemically equivalent. Therefore, benzene exhibits only a singlet peak at δ 7.3 ppm in the 1H NMR spectrum. The observed shift is far downfield because the aromatic ring current strongly deshields the protons. Any substitution on the benzene ring makes the aromatic protons nonequivalent, and the protons split each other. The peak is, therefore, no longer a singlet and the splitting pattern and their associated coupling...
11.3K
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

3.3K
The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...
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Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR
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Collagen Structure-Function Relationships from Solid-State NMR Spectroscopy.

Ieva Goldberga1, Rui Li1, Melinda J Duer1

  • 1Department of Chemistry , University of Cambridge , Lensfield Road , Cambridge CB2 1EW , U.K.

Accounts of Chemical Research
|June 23, 2018
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Summary
This summary is machine-generated.

Solid-state NMR reveals how collagen structure impacts tissue mechanics and disease. It shows glycation stiffens collagen by causing molecular misalignment, not cross-linking, offering new therapeutic avenues.

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Area of Science:

  • Biophysics
  • Biochemistry
  • Materials Science

Background:

  • The extracellular matrix (ECM) is crucial for tissue function, with collagen fibrils providing mechanical support and cell interaction sites.
  • Understanding collagen's molecular structure and its response to stress, aging, and disease is vital for tissue engineering and medicine.
  • Existing knowledge gaps concern how cell-matrix interactions are maintained under stress and how collagen structure changes with age and disease.

Purpose of the Study:

  • To review how solid-state Nuclear Magnetic Resonance (NMR) spectroscopy provides insights into collagen molecular conformation and dynamics.
  • To explore the molecular basis of collagen's mechanical properties and its role in tissue integrity.
  • To investigate the structural changes in collagen associated with aging and disease, particularly glycation.

Main Methods:

  • Solid-state NMR spectroscopy on intact tissues (in vivo and in vitro).
  • In vivo 13C, 15N labeling of the ECM for dynamic and structural analysis.
  • Multidimensional NMR for generating structural 'fingerprints' and comparing local collagen conformation.

Main Results:

  • NMR reveals specific conformations of charged (Lys, Arg) and hydrophobic (Leu, Ile) residues within collagen fibrils, optimizing intermolecular interactions and water exclusion.
  • The abundant Gly-Pro-Hyp triplets confer flexibility to collagen triple helices and fibrils, contrary to expectations of rigidity.
  • Glycation, a non-enzymatic modification, primarily causes side-chain modifications leading to molecular misalignment and fibril stiffening, rather than intermolecular cross-linking.

Conclusions:

  • Solid-state NMR is a powerful tool for elucidating collagen's molecular structure, dynamics, and mechanical properties in native tissues.
  • The flexibility of collagen fibrils is intrinsically linked to the arrangement of Gly-Pro-Hyp triplets, which may protect ligand-binding sites.
  • Collagen stiffening in aging and disease due to glycation results from molecular misalignment, necessitating novel therapeutic strategies targeting this mechanism.