A correspondence between solution-state dynamics of an individual protein and 
the sequence and conformational divertisy of its family.

Friedland, G. D.; Lakomek, N. A.; Griesinger, C.; Meiler, J.; Kortemme, T.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

A correspondence between solution-state dynamics of an individual protein and the sequence and conformational divertisy of its family.

MPS-Authors

/persons/resource/persons15409

Lakomek, N. A.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15147

Griesinger, C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

journal.pcbi.1000393.pdf
(Publisher version), 2MB

Supplementary Material (public)

There is no public supplementary material available

Citation

Friedland, G. D., Lakomek, N. A., Griesinger, C., Meiler, J., & Kortemme, T. (2009). A correspondence between solution-state dynamics of an individual protein and the sequence and conformational divertisy of its family. PLoS Computational Biology, e1000393.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-9381-5

Abstract

There is no abstract available