Alexandros Katranidis
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Explore the profile of Alexandros Katranidis including associated specialties, affiliations and a list of published articles.
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Articles
23
Citations
170
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Recent Articles
11.
Junker N, Vaghefikia F, Albarghash A, Hofig H, Kempe D, Walter J, et al.
J Phys Chem B
. 2019 May;
123(21):4477-4486.
PMID: 31059260
Effects of molecular crowding on structural and dynamical properties of biological macromolecules do depend on the concentration of crowding agents but also on the molecular mass and the structural compactness...
12.
Katranidis A, Fitter J
Anal Chem
. 2019 Jan;
91(4):2570-2576.
PMID: 30648382
Single-molecule techniques are currently an essential tool to study conformational changes as well as the synthesis and folding of proteins. However, the preparation of suitable protein samples is often time-consuming...
13.
Hofig H, Cerminara M, Ritter I, Schone A, Pohl M, Steffen V, et al.
Molecules
. 2018 Nov;
23(12).
PMID: 30486450
Bacterial periplasmic binding proteins (PBPs) undergo a pronounced ligand-induced conformational change which can be employed to monitor ligand concentrations. The most common strategy to take advantage of this conformational change...
14.
Sadoine M, Cerminara M, Gerrits M, Fitter J, Katranidis A
ACS Synth Biol
. 2018 Jan;
7(2):405-411.
PMID: 29370697
Single-molecule FRET (smFRET) is a powerful tool to investigate conformational changes of biological molecules. In general, smFRET studies require protein samples that are site-specifically double-labeled with a pair of donor...
15.
Sadoine M, Cerminara M, Kempf N, Gerrits M, Fitter J, Katranidis A
Anal Chem
. 2017 Oct;
89(21):11278-11285.
PMID: 29022338
Förster resonance energy transfer (FRET) studies performed at the single molecule level have unique abilities to probe molecular structure, dynamics, and function of biological molecules. This technique requires specimens, like...
16.
Wruck F, Katranidis A, Nierhaus K, Buldt G, Hegner M
Proc Natl Acad Sci U S A
. 2017 May;
114(22):E4399-E4407.
PMID: 28507157
Protein biosynthesis is inherently coupled to cotranslational protein folding. Folding of the nascent chain already occurs during synthesis and is mediated by spatial constraints imposed by the ribosomal exit tunnel...
17.
Kempf N, Remes C, Ledesch R, Zuchner T, Hofig H, Ritter I, et al.
Sci Rep
. 2017 Apr;
7:46753.
PMID: 28436469
Cell-free protein synthesis (CFPS) systems were designed to produce proteins with a minimal set of purified components, thus offering the possibility to follow translation as well as protein folding. In...
18.
Tang Y, Dai L, Zhang X, Li J, Hendriks J, Fan X, et al.
Sci Rep
. 2015 Jun;
5:11073.
PMID: 26098742
Single molecule localization based super-resolution fluorescence microscopy offers significantly higher spatial resolution than predicted by Abbe's resolution limit for far field optical microscopy. Such super-resolution images are reconstructed from wide-field...
19.
Gabba M, Poblete S, Rosenkranz T, Katranidis A, Kempe D, Zuchner T, et al.
Biophys J
. 2014 Nov;
107(8):1913-1923.
PMID: 25418172
Over the last few decades, a view has emerged showing that multidomain enzymes are biological machines evolved to harness stochastic kicks of solvent particles into highly directional functional motions. These...
20.
Lamprou P, Kempe D, Katranidis A, Buldt G, Fitter J
Chembiochem
. 2014 Mar;
15(7):977-85.
PMID: 24644265
We report a time-resolved fluorescence anisotropy study of ribosome-bound nascent chains (RNCs) of calmodulin (CaM), a prototypical member of the EF-hand family of calcium-sensing proteins. As shown in numerous studies,...