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Different mechanistic requirements for prokaryotic and eukaryotic chaperonins: a lattice study
Etai Jacob
, Amnon Horovitz
,
R. Unger
The Mina and Everard Goodman Faculty of Life Sciences - at Bar-Ilan University
Research output
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Contribution to journal
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Article
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peer-review
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Keyphrases
Chaperonin
100%
Substrate Proteins
30%
Sequential Change
30%
Protein Folding
20%
Ring Structure
20%
Molecular Chaperone
20%
Cavity Surface
20%
Multidomain Protein
20%
Single Domain Proteins
20%
Conformational Change
10%
Large Population
10%
Mode of Action
10%
Escherichia Coli
10%
Lattice Model
10%
Eukaryotic Cells
10%
Chaperone System
10%
Chaperonin GroEL
10%
Single Domain
10%
Prokaryotes
10%
Functional Consequences
10%
Reaction Cycle
10%
Multi-domain
10%
Static Structure
10%
Cavity Wall
10%
GroEL-GroES
10%
2D Square Lattice
10%
Biochemistry, Genetics and Molecular Biology
Chaperonin
100%
Protein Domain
36%
Surface Property
18%
Conformational Change
9%
GroEL
9%
Protein Folds
9%
GroES
9%
Prokaryote
9%
Protein Folding
9%
Escherichia coli
9%
Adenosine Triphosphate
9%