✦ LIBER ✦

The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer

✍ Scribed by Arthur E. Johnson

Book ID: 116465123
Publisher: Elsevier Science
Year: 2004
Tongue: English
Weight: 101 KB
Volume: 579
Category: Article
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2004.11.046

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Co-Translational Protein Folding on the

Co-Translational Protein Folding on the Ribosome: Using NMR Spectroscopy to Provide Structure and Dynamics of Ribosome-Nascent Chains.

✍ Christodoulou, John 📂 Article 📅 2012 🏛 Biophysical Society 🌐 English ⚖ 40 KB

Co-Translational Protein Folding on the

Co-Translational Protein Folding on the Ribosome: using NMR Spectroscopy to Provide Structure and Dynamics of Ribosome-Nascent Chains

✍ Christodoulou, John 📂 Article 📅 2013 🏛 Biophysical Society 🌐 English ⚖ 42 KB

Full Reconstruction of a Vectorial Prote

Full Reconstruction of a Vectorial Protein Folding Pathway by Afm and Smd: Insights Into the Co-Translational Folding of the Nascent-Polypeptide-Chain

✍ Lee, Whasil; Zeng, Xiancheng; Zhou, Huan-Xiang; Bennett, Vann; Yang, Weitao; Mar 📂 Article 📅 2011 🏛 Biophysical Society 🌐 English ⚖ 38 KB

Fluorescence resonance energy transfer a

Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein

✍ Francis Ka-Ming Chan; Richard M. Siegel; David Zacharias; Ruth Swofford; Kevin L 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 322 KB 👁 2 views

Background: Fluorescence resonance energy transfer (FRET) is a powerful technique for measuring molecular interactions at Ångstrom distances. We present a new method for FRET that utilizes the unique spectral properties of variants of the green fluorescent protein (GFP) for large-scale analysis by f

A Method to Measure the Interaction of R

A Method to Measure the Interaction of Rac/Cdc42 with Their Binding Partners Using Fluorescence Resonance Energy Transfer between Mutants of Green Fluorescent Protein

✍ Debbie L. Graham; Peter N. Lowe; Peter A. Chalk 📂 Article 📅 2001 🏛 Elsevier Science 🌐 English ⚖ 109 KB

Enhanced blue fluorescent protein (EBFP) and enhanced green fluorescent protein (EGFP) mutants of GFP in close proximity to one another can act as a fluorescence resonance energy transfer (FRET) pair. Unstructured amino acid linkers of varying length were inserted between EBFP and EGFP, revealing th

Building-Block Approach for the Straight

Building-Block Approach for the Straightforward Incorporation of a New FRET (Fluorescence-Resonance-Energy Transfer) System into Synthetic DNA

✍ Lilia Clima; Willi Bannwarth 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 German ⚖ 365 KB 👁 1 views

## Abstract The synthesis of the two new phosphoramidites **5** and **8** bearing a carbostyril (=quinolin‐2(1__H__)‐one) chromophore used as donor entity in our recently developed new FRET (fluorescence‐resonance‐energy transfer) system is described (__Schemes 1__ and __2__) The high stability of