Thermodynamics of substrate binding to the chaperone SecB.

No abstract is available for this paper.

• Publication year

  2000

• Venue

  Biochemistry

• Publication date

  2000-02-12

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/BI992065OPMID 10694412
• 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.

• Kinetic mechanism of a partial folding reaction. 2. Nature of the transition state.

  1998cited by this paper
• SecB binds only to a late native-like intermediate in the folding pathway of barstar and not to the unfolded state.

  1998cited by this paper
• Calorimetric analyses of the interaction between SecB and its ligands

  1998cited by this paper
• The interaction between the chaperone SecB and its ligands: Evidence for multiple subsites for binding

  1998cited by this paper
• Structure determination and characterization of Saccharomyces cerevisiae profilin.

  1998cited by this paper
• Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA

  1998cited by this paper
• Specific binding of hoechst 33258 to the d(CGCAAATTTGCG)2 duplex: calorimetric and spectroscopic studies.

  1997cited by this paper
• Calorimetric Observation of a GroEL-Protein Binding Reaction with Little Contribution of Hydrophobic Interaction*

  1997cited by this paper
• Kinetic Partitioning

  1997cited by this paper
• Capturing the misfolds: chaperone-peptide-binding motifs

  1997cited by this paper
• The molecular chaperone SecB is released from the carboxy‐terminus of SecA during initiation of precursor protein translocation

  1997cited by this paper
• The role of water in sequence-independent ligand binding by an oligopeptide transporter protein

  1996cited by this paper
• Molecular chaperones in cellular protein folding

  1996cited by this paper
• Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A.

  1996cited by this paper
• Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

  1996cited by this paper
• High selectivity with low specificity: how SecB has solved the paradox of chaperone binding.

  1995cited by this paper
• Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions.

  1995cited by this paper
• Mapping of the Binding Frame for the Chaperone SecB within a Natural Ligand, Galactose-binding Protein (*)

  1995cited by this paper
• The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands.

  1995cited by this paper
• Thermodynamics of antigen-antibody binding using specific anti-lysozyme antibodies.

  1995cited by this paper
• Chaperone SecB: Conformational changes demonstrated by circular dichroism

  1995cited by this paper
• The Hydrophobic Nature of GroEL-Substrate Binding (*)

  1995cited by this paper
• Protein-peptide interactions.

  1995cited by this paper
• Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB.

  1995cited by this paper
• Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding

  1995cited by this paper
• Structural basis for the binding of proline-rich peptides to SH3 domains.

  1994cited by this paper
• A thermodynamic study of the trp repressor-operator interaction.

  1994cited by this paper
• The structural basis of sequence-independent peptide binding by OppA protein.

  1994cited by this paper
• Determination of the binding frame within a physiological ligand for the chaperone SecB

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

  1994cited by this paper
• Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin.

  1994cited by this paper
• Bound water molecules and conformational stabilization help mediate an antigen-antibody association.

  1994cited by this paper
• Antigenic peptide binding by class I and class II histocompatibility proteins.

  1994cited 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
• Structural basis of pilus subunit recognition by the PapD chaperone.

  1993cited by this paper
• Protein folding in the cell

  1992cited by this paper
• The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC.

  1992cited by this paper
• Peptide binding by chaperone SecB: implications for recognition of nonnative structure.

  1992cited by this paper
• Heat capacity changes for protein-peptide interactions in the ribonuclease S system.

  1992cited by this paper
• A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.

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

  1991cited by this paper
• A critical evaluation of the predicted and X-ray structures of alpha-lactalbumin.

  1990cited by this paper
• ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein.

  1990cited by this paper
• The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.

  1990cited by this paper
• Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme.

  1989cited by this paper
• Rapid measurement of binding constants and heats of binding using a new titration calorimeter.

  1989cited by this paper
• Three pure chaperone proteins of Escherichia coli‐‐SecB, trigger factor and GroEL‐‐form soluble complexes with precursor proteins in vitro.

  1989cited by this paper
• The ‘molten globule’ state is involved in the translocation of proteins across membranes?

  1988cited by this paper
• Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.

  1988cited by this paper
• α‐lactalbumin: compact state with fluctuating tertiary structure?

  1981cited by this paper
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

  1970cited by this paper

• The Sigma-1 Receptor as a Pharmacologic Chaperone: Energetics

  2024cites this paper
• IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below.

  2017cites this paper
• Breaking on through to the other side: protein export through the bacterial Sec system.

  2013cites this paper
• Tight hydrophobic contacts with the SecB chaperone prevent folding of substrate proteins.

  2010cites this paper
• SecB--a chaperone dedicated to protein translocation.

  2010cites this paper
• The interaction of protein disulfide isomerase with a substrate protein at different stages along its folding pathway

  2010cites this paper
• SecB-mediated protein export need not occur via kinetic partitioning.

  2009cites this paper
• Thermodynamics of the protein translocation.

  2009cites this paper
• Effect of crowding agents, signal peptide, and chaperone SecB on the folding and aggregation of E. coli maltose binding protein.

  2009cites this paper
• Chaperone Function in Vitro

  2008cites this paper
• Design, synthesis, and evaluation of linear and cyclic peptide ligands for PDZ10 of the multi-PDZ domain protein MUPP1.

  2007cites this paper
• Single molecule studies on protein translocation in Escherichia coli

  2007cites this paper
• Inactivation of prion proteins via covalent grafting with methoxypoly(ethylene glycol).

  2006cites this paper
• Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein.

  2002cites this paper
• SecB, one small chaperone in the complex milieu of the cell

  2002cites this paper
• Electron Spin Resonance and Fluorescence Studies of the Bound-state Conformation of a Model Protein Substrate to the Chaperone SecB*

  2001cites this paper
• Green Fluorescent Protein variants fold differentially in prokaryotic and eukaryotic cells

  2001influential citation
• Thermodynamics of the folding of D-glyceraldehyde-3-phosphate dehydrogenase assisted by protein disulfide isomerase studied by microcalorimetry.

  2001cites this paper
• Crystal structure of the bacterial protein export chaperone SecB

  2000cites this paper
• The promiscuous and specific sides of SecB

  2000cites this paper
• A Thermodynamic Coupling Mechanism for the Disaggregation of a Model Peptide Substrate by Chaperone SecB*

  2000cites this paper
• Breaking on through to the Other Side: Protein Export through the Bacterial Sec System

  year unknowncites this paper