Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins - Science Advances
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins - Science Advances
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins Science AdvancesIn every established species, protein-protein interactions have evolved such that they are fit for purpose. However, the molecular details of the evolution of new ...
Read here
nmrlearner
Online News
0
04-25-2019 05:39 PM
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins - Science Advances
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins - Science Advances
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins Science AdvancesIn every established species, protein-protein interactions have evolved such that they are fit for purpose. However, the molecular details of the evolution of new ...
Read here
nmrlearner
Online News
0
01-07-2019 05:49 AM
[NMR paper] A General Approach Towards Triazole-linked Adenosine Diphosphate Ribosylated Peptides and Proteins
A General Approach Towards Triazole-linked Adenosine Diphosphate Ribosylated Peptides and Proteins
Current chemistries to prepare Adenosine Diphosphate ribosylated (ADPr) peptides are not generally applicable due to the labile nature of this post-translational modification and its incompatibility with strong acidic conditions used in standard solid phase peptide synthesis protocols. We present a general strategy to prepare ADPr peptide analogues based on a copper catalysed click reaction between an azide modified peptide and an alkyne modified ADPr counterpart. We expand the scope of...
nmrlearner
Journal club
0
12-07-2017 11:34 AM
[NMR paper] The PRE-Derived NMR Model of the 38.8kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests that it Adaptively Recognizes Human Hemoglobin.
The PRE-Derived NMR Model of the 38.8kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests that it Adaptively Recognizes Human Hemoglobin.
Related Articles The PRE-Derived NMR Model of the 38.8kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests that it Adaptively Recognizes Human Hemoglobin.
J Mol Biol. 2015 Feb 13;
Authors: Sjodt M, Macdonald R, Spirig T, Chan AH, Dickson CF, Fabian M, Olson JS, Gell DA, Clubb RT
Abstract
Staphylococcus aureus is a medically important bacterial pathogen that during...
nmrlearner
Journal club
0
02-18-2015 06:15 PM
The PRE-Derived NMR Model of the 38.8kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests that it Adaptively Recognizes Human Hemoglobin
The PRE-Derived NMR Model of the 38.8kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests that it Adaptively Recognizes Human Hemoglobin
Publication date: Available online 14 February 2015
Source:Journal of Molecular Biology</br>
Author(s): Megan Sjodt , Ramsay Macdonald , Thomas Spirig , Albert H. Chan , Claire F. Dickson , Marian Fabian , John S. Olson , David A. Gell , Robert T. Clubb</br>
Staphylococcus aureus is a medically important bacterial pathogen that during infections acquires iron from human hemoglobin (Hb). It uses two closely...