scholarly journals Site-Specific Protein Dynamics Probed by Ultrafast Infrared Spectroscopy of a Noncanonical Amino Acid

2019 ◽  
Vol 123 (45) ◽  
pp. 9592-9597 ◽  
Author(s):  
Christopher R. Hall ◽  
Jinnette Tolentino Collado ◽  
James N. Iuliano ◽  
Agnieszka A. Gil ◽  
Katrin Adamczyk ◽  
...  
Keyword(s):  
Infrared Spectroscopy ◽  
Amino Acid ◽  
Protein Dynamics ◽  
Specific Protein ◽  
Site Specific ◽  
Noncanonical Amino Acid ◽  
Ultrafast Infrared

A noncanonical amino acid-based relay system for site-specific protein labeling

2018 ◽  
Vol 54 (52) ◽  
pp. 7187-7190 ◽  
Author(s):  
Yuda Chen ◽  
Axel Loredo ◽  
Aviva Gordon ◽  
Juan Tang ◽  
Chenfei Yu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Specific Protein ◽  
Protein Labeling ◽  
Relay System ◽  
Site Specific ◽  
Noncanonical Amino Acid

A noncanonical amino acid-based relay system spanning the biosynthesis, incorporation, and bioconjugation of p-aminophenylalanine was developed for site-specific protein labeling.

scholarly journals Site-specific Protein Dynamics in Communication Pathway from Sensor to Signaling Domain of Oxygen Sensor Protein, HemAT-Bs

2012 ◽  
Vol 287 (24) ◽  
pp. 19973-19984 ◽  
Author(s):  
Samir F. El-Mashtoly ◽  
Minoru Kubo ◽  
Yuzong Gu ◽  
Hitomi Sawai ◽  
Satoru Nakashima ◽  
...  
Keyword(s):  
Protein Dynamics ◽  
Oxygen Sensor ◽  
Specific Protein ◽  
Site Specific ◽  
Sensor Protein ◽  
Signaling Domain ◽  
Communication Pathway

Ultrafast Infrared Spectroscopy of Protein Dynamics

1993 ◽  
pp. 517-521 ◽  
Author(s):  
R. M. Hochstrasser ◽  
R. Diller ◽  
S. Maiti ◽  
T. Lian ◽  
B. Locke ◽  
...  
Keyword(s):  
Infrared Spectroscopy ◽  
Protein Dynamics ◽  
Ultrafast Infrared

scholarly journals Two-Dimensional IR Spectroscopy of Protein Dynamics Using Two Vibrational Labels: A Site-Specific Genetically Encoded Unnatural Amino Acid and an Active Site Ligand

2011 ◽  
Vol 115 (38) ◽  
pp. 11294-11304 ◽  
Author(s):  
Megan C. Thielges ◽  
Jun Y. Axup ◽  
Daryl Wong ◽  
Hyun Soo Lee ◽  
Jean K. Chung ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ir Spectroscopy ◽  
Protein Dynamics ◽  
Active Site ◽  
Unnatural Amino Acid ◽  
Two Dimensional ◽  
Site Specific ◽  
A Site

scholarly journals Hydrogen Bond Switching among Flavin and Amino Acid Side Chains in the BLUF Photoreceptor Observed by Ultrafast Infrared Spectroscopy

2008 ◽  
Vol 95 (10) ◽  
pp. 4790-4802 ◽  
Author(s):  
Cosimo Bonetti ◽  
Tilo Mathes ◽  
Ivo H.M. van Stokkum ◽  
Katharine M. Mullen ◽  
Marie-Louise Groot ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Infrared Spectroscopy ◽  
Amino Acid ◽  
Side Chains ◽  
Amino Acid Side Chains ◽  
Ultrafast Infrared

First Site-Specific Incorporation of a Noncanonical Amino Acid into the Photosynthetic Oxygen-Evolving Complex

2014 ◽  
Vol 9 (4) ◽  
pp. 891-896 ◽  
Author(s):  
Adam R. Offenbacher ◽  
Cynthia V. Pagba ◽  
Brandon C. Polander ◽  
Udita Brahmachari ◽  
Bridgette A. Barry
Keyword(s):  
Amino Acid ◽  
Oxygen Evolving Complex ◽  
Site Specific ◽  
Photosynthetic Oxygen ◽  
Oxygen Evolving ◽  
Noncanonical Amino Acid

Systematic Engineering of a Protein Nanocage for High-Yield, Site-Specific Modification

2018 ◽  
Author(s):  
Daniel D. Brauer ◽  
Emily C. Hartman ◽  
Daniel L.V. Bader ◽  
Zoe N. Merz ◽  
Danielle Tullman-Ercek ◽  
...  
Keyword(s):  
Small Molecules ◽  
Protein Modification ◽  
Positive Charge ◽  
Specific Protein ◽  
High Yield ◽  
Site Specific ◽  
Protein Cage ◽  
Protein Carriers ◽  
Site Selective ◽  
Targeted Library

<div> <p>Site-specific protein modification is a widely-used strategy to attach drugs, imaging agents, or other useful small molecules to protein carriers. N-terminal modification is particularly useful as a high-yielding, site-selective modification strategy that can be compatible with a wide array of proteins. However, this modification strategy is incompatible with proteins with buried or sterically-hindered N termini, such as virus-like particles like the well-studied MS2 bacteriophage coat protein. To assess VLPs with improved compatibility with these techniques, we generated a targeted library based on the MS2-derived protein cage with N-terminal proline residues followed by three variable positions. We subjected the library to assembly, heat, and chemical selections, and we identified variants that were modified in high yield with no reduction in thermostability. Positive charge adjacent to the native N terminus is surprisingly beneficial for successful extension, and over 50% of the highest performing variants contained positive charge at this position. Taken together, these studies described nonintuitive design rules governing N-terminal extensions and identified successful extensions with high modification potential.</p> </div>

Sign in / Sign up

Export Citation Format

Share Document