TY - JOUR
T1 - Identification and optimization of protein domains for NMR studies
AU - Card, Paul B.
AU - Gardner, Kevin H.
N1 - Funding Information:
We thank all of the members of the Gardner laboratory for contributing to the development and refinement of these methods within the group. This work has been supported by grants from the National Institutes of Health (CA90601 and CA95471) and the Robert A. Welch Foundation (I-1424) to K.H.G.
PY - 2005
Y1 - 2005
N2 - The success of genomic sequencing projects in recent years has presented protein scientists with a formidable challenge in characterizing the vast number of gene products that have subsequently been identified. NMR has proven to be a valuable tool in the elucidation of various properties for many of these proteins, allowing versatile studies of structure, dynamics, and interactions in the solution state. But the characteristics needed for proteins amenable to this kind of study, such as folding capability, long-term stability, and high solubility, require robust and expeditious methods for the identification and optimization of target protein domains. Here we present a variety of computational and experimental methods developed for these purposes and show that great care must often be taken in the design of constructs intended for NMR-based investigations.
AB - The success of genomic sequencing projects in recent years has presented protein scientists with a formidable challenge in characterizing the vast number of gene products that have subsequently been identified. NMR has proven to be a valuable tool in the elucidation of various properties for many of these proteins, allowing versatile studies of structure, dynamics, and interactions in the solution state. But the characteristics needed for proteins amenable to this kind of study, such as folding capability, long-term stability, and high solubility, require robust and expeditious methods for the identification and optimization of target protein domains. Here we present a variety of computational and experimental methods developed for these purposes and show that great care must often be taken in the design of constructs intended for NMR-based investigations.
UR - http://www.scopus.com/inward/record.url?scp=16244385882&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=16244385882&partnerID=8YFLogxK
U2 - 10.1016/S0076-6879(05)94001-9
DO - 10.1016/S0076-6879(05)94001-9
M3 - Article
C2 - 15808215
AN - SCOPUS:16244385882
SN - 0076-6879
VL - 394
SP - 3
EP - 16
JO - Methods in Enzymology
JF - Methods in Enzymology
ER -