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Related Concept Videos

X-ray Crystallography02:18

X-ray Crystallography

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The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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Structural Protein Function

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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.
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Structural Protein Function

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Fruit Development, Structure, and Function01:58

Fruit Development, Structure, and Function

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Fruits form from a mature flower ovary. As seeds develop from the ovules contained within, the ovary wall undergoes a series of complex changes to form fruit. In some fruits, such as soybeans, the ovary wall dries; in other fruits, such as grapes, it remains fleshy. In some cases, organs other than the ovary contribute to fruit formation; such fruits are called accessory fruits.
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Structure and Function of Erythrocytes01:29

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There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
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Structure and Function of Platelets01:18

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The cell fragments known as platelets are disc-shaped, with an average diameter of about 3 μm and a thickness of roughly 1 μm. They play a crucial role in the body's vascular clotting system, which also involves plasma proteins, blood cells, and blood vessel tissues.
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Methods for Determining and Understanding Serpin Structure and Function: X-Ray Crystallography.

Brian P Mahon1, Robert McKenna2

  • 1Laboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA. bpmahon@princeton.edu.

Methods in Molecular Biology (Clifton, N.J.)
|September 9, 2018
PubMed
Summary
This summary is machine-generated.

X-ray crystallography deciphers serine protease inhibitors (serpins) and their evolutionary history. Emerging methods like cryo-EM will further advance serpin structural biology and medicinal applications.

Keywords:
Cryo-electron microscopyNeutron crystallographySerpin conformationsSerpin structureSmall- and wide-angle solution scatteringX-ray crystallography

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Area of Science:

  • Structural biology
  • Biophysics
  • Protein science

Background:

  • Serine protease inhibitors (serpins) are crucial proteins with diverse biological roles.
  • Understanding serpin structure is key to deciphering their function and inhibitory mechanisms.
  • Serpins have a conserved structure across bacteria, archaea, eukaryotes, and viruses, offering evolutionary insights.

Purpose of the Study:

  • To provide an overview of X-ray crystallography for serpin structural biology.
  • To discuss emerging biophysical techniques for serpin structure determination.
  • To highlight the importance of serpin structural information for future research and drug development.

Main Methods:

  • X-ray crystallography as the predominant method for high-resolution serpin structure determination.
  • Discussion of neutron crystallography, cryo-electron microscopy (cryo-EM), and small- and wide-angle solution scattering (SAXS/WAXS).
  • Integration of structural data to understand serpin evolution and function.

Main Results:

  • X-ray crystallography has yielded significant insights into serpin structure and function.
  • High-resolution structures reveal evolutionary relationships within the serpin superfamily.
  • Emerging methods offer complementary approaches to structural characterization.

Conclusions:

  • Structural studies are vital for understanding serpin biology and medicinal applications.
  • X-ray crystallography remains a cornerstone technique for serpin structural biology.
  • Future applications of advanced biophysical methods will expand our knowledge of this protein family.