Structure of hen lysozyme in solution.

Structure of hen lysozyme in solution.

The structure of the 129-residue protein hen lysozyme has been determined in solution by two-dimensional 1H nuclear magnetic resonance methods. 1158 NOE distance restraints, and 68 phi and 24 chi 1 dihedral angle restraints were employed in conjunction with distance geometry and simulated annealing...

Podrobná bibliografie
Hlavní autoři:	Smith, L, Sutcliffe, M, Redfield, C, Dobson, C
Médium:	Journal article
Jazyk:	English
Vydáno:	1993

Podobné jednotky

Analysis of phi and chi 1 torsion angles for hen lysozyme in solution from 1H NMR spin-spin coupling constants.
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Vydáno: (1991)

A refined solution structure of hen lysozyme determined using residual dipolar coupling data.
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Native-like secondary structure in a peptide from the alpha-domain of hen lysozyme.
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The conformation of lysozyme in solution
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The origin of the alpha-domain intermediate in the folding of hen lysozyme.
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Characterisation of the dominant oxidative folding intermediate of hen lysozyme.
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Vydáno: (1999)

Conformational fluctuations of hen lysozyme investigated by high pressure NMR spectroscopy
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Vydáno: (2003)

Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
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Vydáno: (1994)

Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy.
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Vydáno: (2001)

Insight into a random coil conformation and an isolated helix: structural and dynamical characterisation of the C-helix peptide from hen lysozyme.
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Vydáno: (1996)

Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature.
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Vydáno: (2011)

The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.
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Vydáno: (1999)

Molecular dynamics simulations of peptide fragments from hen lysozyme: insight into non-native protein conformations.
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Vydáno: (1998)

Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
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Vydáno: (2000)

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.
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Vydáno: (2005)

Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes.
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The dynamics of lysozyme from bacteriophage lambda in solution probed by NMR and MD simulations.
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Vydáno: (2013)

Response of native and denatured hen lysozyme to high pressure studied by (15)N/(1)H NMR spectroscopy.
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NMR studies of the dynamics and the folding of hen lysozyme
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Vydáno: (1994)

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Vydáno: (2015-12-01)

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
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Vydáno: (2002)

Oxidative refolding of amyloidogenic variants of human lysozyme.
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Interaction between Sorbitol and Hen Egg White Lysozyme: From Dynamics to Structure
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Prolonged glycation of hen egg white lysozyme generates non amyloidal structures.
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Vydáno: (1999)

Side-chain conformations in an unfolded protein: chi1 distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy.
Autor: Hennig, M, a další
Vydáno: (1999)

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Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain.
Autor: Krebs, MR, a další
Vydáno: (2000)

Expression of recombinant human lysozyme in egg whites of transgenic hens.
Autor: Dainan Cao, a další
Vydáno: (2015-01-01)

Safety evaluation of the food enzyme lysozyme from hens' eggs
Autor: EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), a další
Vydáno: (2023-04-01)

Safety evaluation of the food enzyme lysozyme from hens' eggs
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Vydáno: (2023-03-01)

Molecular dynamics simulation or structure refinement of proteins: are solvent molecules required? a case study using hen lysozyme
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Vydáno: (2022)

Structure of hen egg-white lysozyme solvated in TFE/water: a molecular dynamics simulation study based on NMR data.
Autor: Eichenberger, A, a další
Vydáno: (2013)

Structure of hen egg-white lysozyme solvated in TFE/water: a molecular dynamics simulation study based on NMR data
Autor: Eichenberger, A, a další
Vydáno: (2013)

Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme.
Autor: Morozova-Roche, L, a další
Vydáno: (1999)

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
Autor: Dumoulin, M, a další
Vydáno: (2005)

Research advancements in the purification technology and application of hen egg white lysozyme
Autor: Liang-Liang Chen, a další
Vydáno: (2024-12-01)