Plasticity and transient binding are key ingredients of the periplasmic chaperone network.

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Bibliographic Details
Title: Plasticity and transient binding are key ingredients of the periplasmic chaperone network.
Authors: Chum AP; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland., Shoemaker SR; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland., Fleming PJ; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland., Fleming KG; T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland.
Source: Protein science : a publication of the Protein Society [Protein Sci] 2019 Jul; Vol. 28 (7), pp. 1340-1349. Date of Electronic Publication: 2019 May 23.
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
Journal Info: Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1469-896X (Electronic) Linking ISSN: 09618368 NLM ISO Abbreviation: Protein Sci Subsets: MEDLINE
Database: MEDLINE Ultimate
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ISSN:1469-896X
DOI:10.1002/pro.3641