(Q47590925)

4 February 2018

title

Intra-molecular chaperone: the role of the N-terminal in conformational selection and kinetic control (English)

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4 February 2018

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2

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4 February 2018

Ruth Nussinov

series ordinal

3

object named as

Ruth Nussinov

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4 February 2018

1

Chung-Jung Tsai

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4 February 2018

publication date

4 February 2009

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4 February 2018

published in

Physical Biology

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4 February 2018

volume

6

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4 February 2018

issue

1

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4 February 2018

page(s)

013001

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4 February 2018

A protein-folding reaction under kinetic control

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Sucrase is an intramolecular chaperone located at the C-terminal end of the sucrase-isomaltase enzyme complex

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The prosequence of human lactase-phlorizin hydrolase modulates the folding of the mature enzyme

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Intermediate states in protein folding

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Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability

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A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

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Protein folding and function: the N-terminal fragment in adenylate kinase

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Synonymous mutations and ribosome stalling can lead to altered folding pathways and distinct minima

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Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins.

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Structure of Microcin J25, a Peptide Inhibitor of Bacterial RNA Polymerase, is a Lassoed Tail

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C-terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?

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The building block folding model and the kinetics of protein folding

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Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure.

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Folding pathway mediated by an intramolecular chaperone: characterization of the structural changes in pro-subtilisin E coincident with autoprocessing

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The energy landscapes of repeat-containing proteins: topology, cooperativity, and the folding funnels of one-dimensional architectures

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Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding

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Reassembly of active caspase-3 is facilitated by the propeptide

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12 December 2020

Protein folding and misfolding: mechanism and principles.

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Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot

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12 December 2020

10.1088/1478-3975/6/1/013001

Identifiers

DOI

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4 February 2018

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4 February 2018