Native-like tertiary structure formation in the alpha-domain of a hen lysozyme two-disulfide variant.

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Journal of Molecular Biology

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  PMID 11718564
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• A comparative study of peptide models of the alpha-domain of alpha-lactalbumin, lysozyme, and alpha-lactalbumin/lysozyme chimeras allows the elucidation of critical factors that contribute to the ability to form stable partially folded states.

  2001cited by this paper
• Response of native and denatured hen lysozyme to high pressure studied by (15)N/(1)H NMR spectroscopy.

  2001cited by this paper
• The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge.

  2000cited by this paper
• Propensities for the formation of individual disulfide bonds in hen lysozyme and the size and stability of disulfide‐associated submolecular structures

  2000cited by this paper
• Distribution of disulfide bonds in the two-disulfide intermediates in the regeneration of bovine pancreatic ribonuclease A: further insights into the folding process.

  1999cited by this paper
• Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A.

  1996cited by this paper
• Energetics of structural domains in α‐lactalbumin

  1996cited by this paper
• Bipartite structure of the alpha-lactalbumin molten globule.

  1995cited by this paper
• Local structural preferences in the alpha-lactalbumin molten globule.

  1995cited by this paper
• The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozyme.

  1995cited by this paper
• Energetics of the alpha-lactalbumin states: a calorimetric and statistical thermodynamic study.

  1994cited by this paper
• A protein dissection study of a molten globule.

  1994cited by this paper
• Disulfide-rearranged molten globule state of alpha-lactalbumin.

  1994cited by this paper
• Relationship between the optimal temperature for oxidative refolding and the thermal stability of refolded state of hen lysozyme three-disulfide derivatives.

  1994cited by this paper
• Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.

  1993cited by this paper
• Synthesis of a fluorescent derivatizing reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography.

  1993cited by this paper
• Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin.

  1993cited by this paper
• Pathway of disulfide-coupled unfolding and refolding of bovine alpha-lactalbumin.

  1993cited by this paper
• Structure of hen lysozyme in solution.

  1993cited by this paper
• Efficient in vitro folding of the three‐disulfide derivatives of hen lysozyme in the presence of glycerol

  1992cited by this paper
• Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond.

  1992cited by this paper
• Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme.

  1992cited by this paper
• The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.

  1992cited by this paper
• The folding of hen lysozyme involves partially structured intermediates and multiple pathways

  1992cited by this paper
• Demonstration by NMR of folding domains in lysozyme

  1991cited by this paper
• (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study.

  1991cited by this paper
• The molten globule protein conformation probed by disulphide bonds

  1991cited by this paper
• Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor.

  1991cited by this paper
• Structural effects induced by removal of a disulfide-bridge: the X-ray structure of the C30A/C51A mutant of basic pancreatic trypsin inhibitor at 1.6 A.

  1990cited by this paper
• Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds.

  1988cited by this paper
• Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution.

  1988cited by this paper
• Influence of an extrinsic cross-link on the folding pathway of ribonuclease A. Conformational and thermodynamic analysis of cross-linked (lysine7-lysine41)-ribonuclease a.

  1984cited by this paper
• Two-dimensional 1H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor. Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein.

  1984cited by this paper
• A new two-disulphide intermediate in the refolding of reduced bovine pancreatic trypsin inhibitor.

  1984cited by this paper
• Proline-specific endopeptidase from Flavobacterium. Purification and properties.

  1980cited by this paper
• Conformational stability of ribonuclease T1. II. Salt-induced renaturation.

  1979cited by this paper
• Formation of the four isomers of hen egg white lysozyme containing three negative disulfide bonds and one open disulfide bond.

  1977cited by this paper
• A study of renaturation of reduced hen egg white lysozyme. Enzymically active intermediates formed during oxidation of the reduced protein.

  1976cited by this paper
• A tryptophyl circular dichroic band at 305 mu of hen egg-white lysozyme.

  1972cited by this paper
• Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme.

  1970cited by this paper
• The binding of N-acetylglucosamine to lysozyme. Studies on circular dichroism.

  1969cited by this paper
• Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.

  1965cited by this paper

• Synthetic liposomal mimics of biological viruses for the study of immune responses to infection and vaccination.

  2020cites this paper
• Glycerol‐induced folding of unstructured disulfide‐deficient lysozyme into a native‐like conformation

  2009cites this paper
• Comprehensive secondary‐structure analysis of disulfide variants of lysozyme by synchrotron‐radiation vacuum‐ultraviolet circular dichroism

  2009cites this paper
• Coarse grain molecular dynamics simulation for the prediction of tertiary conformation of lysozyme adsorbed on silica surface

  2009cites this paper
• Stability of hen egg white lysozyme during denaturation is enhanced by pretreatment with supercritical carbon dioxide.

  2009cites this paper
• Effect of surface concentration on secondary and tertiary conformational changes of lysozyme adsorbed on silica nanoparticles.

  2008cites this paper
• Characterisation of Disulfide‐Bond Dynamics in Non‐Native States of Lysozyme and Its Disulfide Deletion Mutants by NMR

  2005cites this paper
• Hierarchical map of protein unfolding and refolding at thermal equilibrium revealed by wide-angle X-ray scattering.

  2004cites this paper
• NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins.

  2004cites this paper
• Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils

  2004cites this paper
• Immunochemical pulsed‐labeling characterization of intermediates during hen lysozyme oxidative folding

  2002cites this paper
• Role of individual disulfide bonds in hen lysozyme early folding steps

  2002cites this paper
• NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.

  2002cites this paper