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Biochemistry, Biophysics, and Structural Biology

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2017

Protein dynamics

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Full-Text Articles in Life Sciences

The Glycosyltransferases Of Lps Core: A Review Of Four Heptosyltransferase Enzymes In Context, Erika A. Taylor Sep 2017

The Glycosyltransferases Of Lps Core: A Review Of Four Heptosyltransferase Enzymes In Context, Erika A. Taylor

Erika A. Taylor, Ph.D.

Bacterial antibiotic resistance is a rapidly expanding problem in the world today.
Functionalization of the outer membrane of Gram-negative bacteria provides protection from
extracellular antimicrobials, and serves as an innate resistance mechanism. Lipopolysaccharides (LPS)
are a major cell-surface component of Gram-negative bacteria that contribute to protecting the
bacteriumfromextracellular threats. LPS is biosynthesized by the sequential addition of sugarmoieties
by a number of glycosyltransferases (GTs). Heptosyltransferases catalyze the addition of multiple
heptose sugars to form the core region of LPS; there are at most four heptosyltransferases found in
all Gram-negative bacteria. The most studied of the four is HepI. Cells deficient …

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Exploring The Physics Of Proteins At Molecular Level By Neutron And X-Ray Scattering, Utsab Raj Shrestha Jan 2017

Exploring The Physics Of Proteins At Molecular Level By Neutron And X-Ray Scattering, Utsab Raj Shrestha

Wayne State University Dissertations

The protein structures revealed by the crystallographic studies have provided the valuable information over the years regarding their biological functions. However, such snapshots of protein fluctuations averaged over time may not be enough to fully capture the underlying biological phenomena. A deeper understanding of the protein dynamics is crucial for elucidating the structural pathways or the transition mechanism from the initial state to the final state necessary for regulating the physical and chemical processes. Hence, the biological activities and functions are mainly governed by the protein conformational dynamics. However, the direct correlation of a wide range of protein dynamics to …

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The Stories Tryptophans Tell: Exploring Protein Dynamics Of Heptosyltransferase I From Escherichia Coli, Erika A. Taylor Dec 2016

The Stories Tryptophans Tell: Exploring Protein Dynamics Of Heptosyltransferase I From Escherichia Coli, Erika A. Taylor

Erika A. Taylor, Ph.D.

Heptosyltransferase I (HepI) catalyzes the addition of L-glycero-β-Dmanno-heptose to Kdo2-Lipid A, as part of the biosynthesis of the core region of lipopolysaccharide (LPS). Gram-negative bacteria with gene knockouts of HepI have reduced virulence and enhanced susceptibility to hydrophobic antibiotics, making the design of inhibitors of HepI of interest. Because HepI protein dynamics are partially ratelimiting, disruption of protein dynamics might provide a new strategy for inhibiting HepI. Discerning the global mechanism of HepI is anticipated to aid development of inhibitors of LPS biosynthesis. Herein, dynamic protein rearrangements involved in the HepI catalytic cycle were probed by combining mutagenesis with intrinsic …

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