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Chaperone

Most reactions in cells are carried out by enzymes [1], In many instances the rates of enzyme-catalysed reactions are enhanced by a factor of a million. A significantly large fraction of all known enzymes are proteins which are made from twenty naturally occurring amino acids. The amino acids are linked by peptide bonds to fonn polypeptide chains. The primary sequence of a protein specifies the linear order in which the amino acids are linked. To carry out the catalytic activity the linear sequence has to fold to a well defined tliree-dimensional (3D) stmcture. In cells only a relatively small fraction of proteins require assistance from chaperones (helper proteins) [2]. Even in the complicated cellular environment most proteins fold spontaneously upon synthesis. The detennination of the 3D folded stmcture from the one-dimensional primary sequence is the most popular protein folding problem. [Pg.2642]

How does the GroEL-GroES complex function as a chaperone to assist protein folding Although several aspects of the mechanism are not clear, the main features of the functional cycle are known. The first step is the... [Pg.102]

Hartl, F.U. Molecular chaperones in cellular protein folding. Nature 381 571-580, 1996. [Pg.119]

Zhu, X., et al. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272 1606-1614, 1996. [Pg.120]

Molecular Chaperones Proteins That Help Fold Glohular Proteins... [Pg.191]

The way in which molecular chaperones interact with polypeptides during the folding process is not completely understood. What is clear is that chaperones bind effectively to the exposed hydrophobic regions of partially folded structures. These folding intermediates are less compact than the native folded proteins. They contain large amounts of secondary and even some tertiary... [Pg.192]

FIGURE 6.36 A model for the steps involved in the folding of globular proteins. Chaperone proteins may assist in the initiation of the folding process. [Pg.193]

Flynn, G. C., Beckers, C. J. M., Baase, W. A., and Dahlquist, F. W. (1993). Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones. Proc. Natl. Acad. Sci. USA 90 10826-10830. [Pg.395]

Molecular chaperone (relative molecular mass 78 K) found in the lumen of the ER. BiP is related to the Hsp70 family of heat-shock proteins and was originally described as immunoglobulin heavy chain binding protein. [Pg.271]

Molecular chaperones, stress proteins (note not all stress proteins are molecular chaperones and not all molecular chaperones are stress proteins) Heat shock proteins (Hsp) Polypeptide chain binding proteins... [Pg.347]

Chaperones bind to exposed hydrophobic surfaces of polypeptide substrates, and through either ATP-dependent or ATP-independent mechanisms facilitate the folding/assembly, intracellular transport, degradation, and activity of polypeptides. [Pg.347]

The term molecular chaperone was coined by Ron A. Laskey and coworkers in 1978 to describe the... [Pg.347]

Today, molecular chaperones are divided into three principle classes, according to their mode of action (Table 1). The one class comprises the chaperonins or HsplOO protein family members. Chaperonins are oligomeric proteins, composed of two rings placed... [Pg.348]

Chaperones. Table 1 Molecular Chaperones in Humans (note this list is not meant to be exhaustive). Synonyms are given in parentheses... [Pg.348]

Co-chaperones of Hsp60 Prefold in (GimC) - Cpn10 (mtHspIO)... [Pg.348]

As it is the case in polypeptide folding, nonspecific or promiscuous RNA-binding proteins can prevent RNA mis-folding and resolve mis-foldedRNAs, thereby ensuring that RNA is accessible for its biological function [ 1 ]. Certain DEAD-box proteins as well as some proteins that are involved in the assembly of ribonuleoparticles were shown to act as RNA chaperones. [Pg.349]

Chaperones. Figure 2 The multiple roles of BiP in the biogenesis of the secretory proteins. BiP, immunoglobulin heavy chain binding protein ER, endoplasmic reticulum ERAD, ER-associated degradation ERj, resident ER protein with J-domain Sec61, core subunit of the protein translocase UPR, unfolded protein response that involves several signal transduction pathways that are activated in order to increase the biosynthetic capacity and decrease the biosynthetic burden of the ER... [Pg.350]


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ATPases chaperone activity

Amyloid proteins chaperone effect

Assembly reactions chaperone proteins

Autophagy chaperon-mediated

Biological Factor Chaperones

Chaperon effect

Chaperon ins

Chaperon mechanism

Chaperon molecule

Chaperone 320 Subject

Chaperone GroEL

Chaperone GroES

Chaperone calnexin

Chaperone effect

Chaperone efficiencies, in reaction

Chaperone heat shock proteins

Chaperone molecules

Chaperone molecules chemical chaperones

Chaperone molecules heat shock proteins

Chaperone molecules models

Chaperone molecules protein

Chaperone peptides

Chaperone proteins

Chaperone proteins chaperonins)

Chaperone proteins, apoE function

Chaperone proteins, mitochondria

Chaperone-like Activity

Chaperone-mediated autophagy

Chaperone-mediated folding

Chaperone/usher pathway

Chaperone:adhesin complex

Chaperoned strategy

Chaperones 3 strands

Chaperones ATPase activity

Chaperones Atxl-like

Chaperones DnaK/DnaJ

Chaperones Hsp70-binding protein

Chaperones binding capacity

Chaperones bound, nature

Chaperones characterization

Chaperones consensus sequences

Chaperones delivery pathways

Chaperones discovery

Chaperones endoplasmic reticulum

Chaperones folding pathway

Chaperones for Copper-Zinc Superoxide Dismutase

Chaperones for cytochrome c oxidase

Chaperones function

Chaperones function, regulation

Chaperones heat-shock response molecular

Chaperones histone

Chaperones homologues, structure

Chaperones identification

Chaperones metal transfer mechanism

Chaperones model

Chaperones of Mammals

Chaperones overview

Chaperones pilus

Chaperones protein fold

Chaperones small Hsps

Chaperones structure

Chaperones structure, determination

Chaperones substrate binding site

Chaperones substrate complexes

Chaperones substrate conformation

Chaperones substrate recognition

Chaperones substrate release

Chaperones substrate unfolding

Chaperones trigger factor

Chaperones tubulin specific

Chaperons

Chaperons

Chemical chaperone therapy

Chemical chaperones

Chemical/pharmacological chaperone

Chemical/pharmacological chaperone strategies

Co-chaperone

Collagen molecular chaperon

Conformations chemical chaperones

Conformations molecular chaperones role

Copper chaperone for superoxide dismutase

Copper chaperones

Cytoplasmic copper chaperone

Cytosolic protein folding molecular chaperones

GroEL/GroES molecular chaperone machine

HSP90 molecular chaperone

Heat shock protein chaperone interaction

Heat shock proteins molecular chaperone role

Hsp Chaperone Activity

Hsp70 molecular chaperone

Hsp70 molecular chaperone system

Inclusion chaperones

Intramolecular Chaperone of Endosialidase

Lactam-like Chaperone Inhibitors

Lipid chaperone

Metal chaperones

Models sHsp chaperone

Molecular chaperones

Molecular chaperones DnaK/DnaJ

Molecular chaperones definitions

Molecular chaperones discovery

Molecular chaperones heat-shock proteins

Molecular chaperones maturation

Molecular chaperones molecules

Molecular chaperones response

Nitration chaperon effect

PapD chaperone

Periplasmic pilus chaperone protein

Pharmacological Chaperone Therapy

Pharmacological chaperones

Protein Folding Chaperoned and Unchaperoned

Protein folding chaperone proteins

Protein folding chaperons

Protein folding chaperons proteins

Protein folding molecular chaperones

Protein molecular chaperone role

Protein targeting chaperones

Protein-Folding Chaperones

Quality control chaperones

Secretion chaperones

Solvent chaperoned

Stress protein molecular chaperones

Structure, three-dimensional chaperones

The DegP Protease Chaperone A Molecular Cage with Bouncers

The Targeting Activity of Co-chaperones

Yeast prions chaperones

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