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250 Aktuelle Fachpublikationen zum Thema Addition

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Quantification of Quaternary Structure Stability in Aggregation-Prone Proteins under Physiological Conditions: The Transthyretin Case

07.10.2014 | Lei Z. Robinson; Natàlia Reixach, Biochemistry, 2014

The quaternary structure stability of proteins is typically studied under conditions that accelerate their aggregation/unfolding processes on convenient laboratory time scales. Such conditions include high temperature or pressure, chaotrope-mediated unfolding, or low or high pH. These approaches ...


Crystal Structure of Psb31, a Novel Extrinsic Protein of Photosystem II from a Marine Centric Diatom and Implications for Its Binding and Function

11.09.2013 | Ryo Nagao; Michihiro Suga; Ayako Niikura; Akinori Okumura; Faisal Hammad Mekky Koua; Takehiro Suzuki; Tatsuya Tomo; ..., Biochemistry, 2013

Psb31 is a fifth extrinsic protein found in photosystem II (PSII) of a centric diatom, Chaetoceros gracilis. The protein has been shown to bind directly to PSII in the absence of other extrinsic proteins and serves in part as a substitute for PsbO in supporting oxygen evolution. We report here ...


Localized Permeabilization of E. coli Membranes by the Antimicrobial Peptide Cecropin A

10.09.2013 | Nambirajan Rangarajan; Somenath Bakshi; James C. Weisshaar, Biochemistry, 2013

Fluorescence microscopy enables detailed observation of the effects of the antimicrobial peptide Cecropin A on the outer membrane (OM) and cytoplasmic membrane (CM) of single E. coli cells with subsecond time resolution. Fluorescence from periplasmic GFP decays and cell growth halts when the OM ...


Binding of Chondroitin 4-Sulfate to Cathepsin S Regulates Its Enzymatic Activity

04.09.2013 | Juliette Sage; Florian Mallèvre; Fabien Barbarin-Costes; Sergey A. Samsonov; Jan-Philip Gehrcke; Maria Teresa Pisaba ..., Biochemistry, 2013

Human cysteine cathepsin S (catS) participates in distinct physiological and pathophysiological cellular processes and is considered as a valuable therapeutic target in autoimmune diseases, cancer, atherosclerosis, and asthma. We evaluated the capacity of negatively charged glycosaminoglycans ...


Contribution of Electrostatics to the Binding of Pancreatic-Type Ribonucleases to Membranes

30.08.2013 | Nadia K. Sundlass; Chelcie H. Eller; Qiang Cui; Ronald T. Raines, Biochemistry, 2013

Pancreatic-type ribonucleases show clinical promise as chemotherapeutic agents but are limited in efficacy by the inefficiency of their uptake by human cells. Cellular uptake can be increased by the addition of positive charges to the surface of ribonucleases, either by site-directed mutagenesis ...


Carboxyl Group of Glu113 Is Required for Stabilization of the Diferrous and Bis-FeIV States of MauG

30.08.2013 | Nafez Abu Tarboush; Erik T. Yukl; Sooim Shin; Manliang Feng; Carrie M. Wilmot; Victor L. Davidson, Biochemistry, 2013

The diheme enzyme MauG catalyzes a six-electron oxidation required for post-translational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Crystallographic studies have implicated ...


What’s in Your Buffer? Solute Altered Millisecond Motions Detected by Solution NMR

30.08.2013 | Madeline Wong; Gennady Khirich; J. Patrick Loria, Biochemistry, 2013

To date, little work has been conducted on the relationship between solute and buffer molecules and conformational exchange motion in enzymes. This study uses solution NMR to examine the effects of phosphate, sulfate, and acetate in comparison to MES- and HEPES-buffered references on the chemical ...


Interaction of Nonstructural Protein 5A of the Hepatitis C Virus with Src Homology 3 Domains Using Noncanonical Binding Sites

26.08.2013 | Melanie Schwarten; Zsófia Sólyom; Sophie Feuerstein; Amine Aladağ; Silke Hoffmann; Dieter Willbold; Bernhard Brutscher, Biochemistry, 2013

Src homology 3 (SH3) domains are widely known for their ability to interact with other proteins using the canonical PxxP binding motif. Besides those well-characterized interaction modes, there is an increasing number of SH3 domain-containing complexes that lack this motif. Here we characterize ...


Structural Studies of Hydroxylamine Oxidoreductase Reveal a Unique Heme Cofactor and a Previously Unidentified Interaction Partner

26.08.2013 | Peder Cedervall; Alan B. Hooper; Carrie M. Wilmot, Biochemistry, 2013

Hydroxylamine oxidoreductase (HAO) is a 24-heme homotrimeric enzyme that catalyzes the conversion of hydroxylamine to nitrite in nitrifying bacteria: a key reaction in the nitrogen cycle. One heme in each HAO monomer is a highly unusual heme P460 that is the site of catalysis. This was proposed ...


Resonance Raman Characterization of the Ammonia-Generated Oxo Intermediate of Cytochrome c Oxidase from Paracoccus denitrificans

23.08.2013 | Jacek Kozuch; Iris von der Hocht; Florian Hilbers; Hartmut Michel; Inez M. Weidinger, Biochemistry, 2013

A novel oxo state of cytochrome c oxidase from Paracoccus denitrificans generated by successive addition of excess H2O2 and ammonia was investigated using resonance Raman (RR) spectroscopy. Addition of ammonia to the H2O2-generated artificial F state resulted in an upshift of the oxoferryl ...


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