The early history of lysozyme

@article{Johnson1998TheEH,
  title={The early history of lysozyme},
  author={Louise N. Johnson},
  journal={Nature Structural Biology},
  year={1998},
  volume={5},
  pages={942-944}
}
  • L. Johnson
  • Published 1 November 1998
  • Chemistry, Biology
  • Nature Structural Biology
struct used by Rayment at al., and in addition have solved both constructs with ADP.AlF4 bound. In each case they obtain the closed form. Since the crystal forms obtained display a wealth of non-crystallographic symmetry, the closed conformation has now been found 17 times. Little doubt can remain that the closed form represents a biological significant second conformation of the myosin cross bridge. As a bonus, the smooth muscle construct with one light chain (Fig. 2) shows that the light… 
Biography of Martha L. Ludwig.
  • E. Hitt
  • Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2004
In 1965, lysozyme became the first three-dimensional enzyme structure to be solved with x-ray crystallography (1). At the time, Martha L. Ludwig was a young research fellow at Harvard University
The Chitopentaose Complex of a Mutant Hen Egg-White Lysozyme Displays No Distortion of the –1 Sugar Away from a 4C1 Chair Conformation
TLDR
It is shown that the chitopentaose product complex of a mutant E35Q HEWL, solved at 1.8 A resolution, is bound with all sugars in 4C1 conformation.
REFOLDING KINETICS OF LYSOZYME: NUCLEAR MAGNETIC RESONANCE & MOLECULAR DYNAMICS STUDY OF HEN EGG-WHITE LYSOZYME by ÇET
TLDR
The results supported previous interpretations that a protein fingerprint exists, which make out distinct intermediates forming along the unfolding pathways of native hen egg-white lysozyme.
Measuring elastic properties of a protein monolayer at water surface by lateral compression
A protein monolayer grown at a water surface decorated with a mild coverage of surfactants, was compressed laterally followed by decompression in a cycle. The surface tension and the thickness of the
Small Angle Neutron Scattering studies of Lysozyme solutions
Biomolecules such as proteins or nucleic acids are polymers that sustain life, with unique structures and broad scale dynamics. Inherent to their complexity, and ability to function in a variety of
A chemical, structural and biophysical exploration into the nanoscale properties of amyloid fibrils
TLDR
It has been demonstrated that polymer rigidity (Lp) is inherently linked to the resistance of the tested amyloid fibrils to mechanical stress.
Exploring free energy landscapes of large conformational changes: molecular dynamics with excited normal modes.
TLDR
The MDeNM (molecular dynamics with excited normal modes) method presented here consists of multiple-replica short MD simulations in which motions described by a given subset of low-frequency NMs are kinetically excited, thus allowing an efficient coupling between slow and fast motions.
Thermal motions quantification of lysozyme in aqueous mixtures with different co-solvent: glycerol [C3H5(OH)3], trehalose [C12H22O11], sucrose [C12H22O11], and a chaotropic agent [CO(NH2)2] by osiris near-backscattering crystal analyser spectrometer
Thermal neutron scattering is a powerful tool to directly probe protein internal motions. Here, we report an incoherent neutron scattering study of the effect of glycerol-, disaccharide-
Dame Louise Napier Johnson. 26 September 1940—25 September 2012
Louise Johnson was a leading architect of protein crystallography and structural enzymology. She pioneered the application of the technique to understand how enzymes function at the molecular level.
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References

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Crystallographic studies of the activity of hen egg-white lysozyme
The chemical evidence for the enzymic activity of lysozyme will be discussed in detail by other speakers at this meeting, but in order to describe our crystallographic studies of the interactions
The chemical structure of lysozyme substrates and their cleavage by the enzyme
  • N. Sharon
  • Chemistry, Biology
    Proceedings of the Royal Society of London. Series B. Biological Sciences
  • 1967
TLDR
It is proposed that hydrolysis of the tetrasaccharide does not proceed by direct cleavage, but by a transfer mechanism, via long chain oligosaccharides, viaLong chain oligoseccharides strongly inhibit the enzymic activity of lysozyme.
The binding and cleavage by lysozyme of N-acetylglucosamine oligosaccharides
  • J. A. Rupley
  • Chemistry
    Proceedings of the Royal Society of London. Series B. Biological Sciences
  • 1967
TLDR
This paper describes reactions of certain lysozymesaccharides of N -acetylglucosamine, namely, their binding and cleavage by the enzyme.
The Binding and Cleavage by Lysozyme of N-acetylglucosamine Oligosaccharides
In the first part of this Discussion the beautiful crystallographic results obtained at the Royal Institution were described (Blake, Mair et al ., p. 365, Blake, Johnson et al ., p. 378). Particular
The mechanisms of hydrolysis of glycosides and their revelance to enzyme-catalysed reactions.
TLDR
Glycoside hydrolysis can be formally represented by (I), where the group O R is displaced from the C1 or C2 atom of an aldose or ketose sugar (or sugar derivative) respectively; the ring system being either five- or six-membered.
Structure Of Lysozyme: A Fourier Map of the Electron Density at 6 Å Resolution obtained by X-ray Diffraction
Structure Of Lysozyme: A Fourier Map of the Electron Density at 6 A Resolution obtained by X-ray Diffraction
Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å Resolution
Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution
The Eigth Day of Creation, (Simon
  • 1979
Social Change and Scientific Organisation: The Royal Institution
  • 1978
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