Resolving dual binding conformations of cellulosome cohesin-dockerin complexes using single-molecule force spectroscopy.
about
The length but not the sequence of peptide linker modules exerts the primary influence on the conformations of protein domains in cellulosome multi-enzyme complexes.Global Distribution Patterns and Pangenomic Diversity of the Candidate Phylum "Latescibacteria" (WS3).The influence of disulfide bonds on the mechanical stability of proteins is context dependent.Biasing effects of receptor-ligand complexes on protein-unfolding statistics.Dual binding mode in cohesin-dockerin complexes as assessed through stretching studies.Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module.Ligand Binding Stabilizes Cellulosomal Cohesins as Revealed by AFM-based Single-Molecule Force Spectroscopy.
P2860
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P2860
Resolving dual binding conformations of cellulosome cohesin-dockerin complexes using single-molecule force spectroscopy.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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name
Resolving dual binding conform ...... e-molecule force spectroscopy.
@ast
Resolving dual binding conform ...... e-molecule force spectroscopy.
@en
type
label
Resolving dual binding conform ...... e-molecule force spectroscopy.
@ast
Resolving dual binding conform ...... e-molecule force spectroscopy.
@en
prefLabel
Resolving dual binding conform ...... e-molecule force spectroscopy.
@ast
Resolving dual binding conform ...... e-molecule force spectroscopy.
@en
P2093
P2860
P356
P1433
P1476
Resolving dual binding conform ...... le-molecule force spectroscopy
@en
P2093
Constantin Schoeler
Daniel B Fried
Edward A Bayer
Hermann E Gaub
Markus A Jobst
Michael A Nash
Wolfgang Ott
P2860
P356
10.7554/ELIFE.10319
P407
P577
2015-10-31T00:00:00Z