In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.

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The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli.

P2860

Q33719566-5DDD486C-32D6-4EA1-B848-91C840E8EE1D

P2860

In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.

Item

http://www.wikidata.org/entity/Q36640559

description

2001 nî lūn-bûn

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2001年の論文

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2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

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2001年論文

@zh-tw

2001年论文

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2001年论文

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2001年论文

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name

In vivo assembly of aspartate ...... catalytic polypeptide chains.

@ast

In vivo assembly of aspartate ...... catalytic polypeptide chains.

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type

Item

label

In vivo assembly of aspartate ...... catalytic polypeptide chains.

@ast

In vivo assembly of aspartate ...... catalytic polypeptide chains.

@en

prefLabel

In vivo assembly of aspartate ...... catalytic polypeptide chains.

@ast

In vivo assembly of aspartate ...... catalytic polypeptide chains.

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P1476

In vivo assembly of aspartate ...... catalytic polypeptide chains.

@en

P2093

H K Schachman

http://www.w3.org/2001/XMLSchema#string

X Ni

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P2860

Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor

Different folding transition states may result in the same native structure

In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly

Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function

ON THE ENZYMIC ACTIVITY OF SUBTILISIN-MODIFIED RIBONUCLEASE

Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms

The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics

Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis

Circularly permuted beta-lactamase from Staphylococcus aureus PC1

The preparation of subtilisn-modified ribonuclease and the separation of the peptide and protein components

P304

519-527

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scholarly article

P356

10.1110/PS.38901

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2001-03-01T00:00:00Z

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227866382

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P698

11344320

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P921

cyclic permutation

P932

2374128

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In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.

about

P2860

P2860

In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932