2004
DOI: 10.1002/ange.200460629
|View full text |Cite
|
Sign up to set email alerts
|

Design of a Conformation‐Sensitive Xenon‐Binding Cavity in the Ribose‐Binding Protein

Abstract: 129Xe‐NMR‐Spektroskopie trifft Protein‐Engineering: NMR‐Spektroskopie mit Laser‐polarisiertem 129Xe hilft nur beim Nachweis von Proteinkonformationen, wenn das Protein über eine konformativ empfindliche Xenon bindende Kavität verfügt. Diese fehlt jedoch vielen Proteinen. Der vorgestellte Designprozess führte zu einer entsprechenden Kavität im Ribose bindenden Protein (siehe Bild) und damit zum 129Xe‐NMR‐spektroskopischen Nachweis von Proteinkonformation und Ligandenbindung.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

1
14
0

Year Published

2007
2007
2016
2016

Publication Types

Select...
8

Relationship

1
7

Authors

Journals

citations
Cited by 10 publications
(16 citation statements)
references
References 20 publications
1
14
0
Order By: Relevance
“…Xenon binding to myoglobin has been well characterized by NMR spectroscopy (43,44) and X-ray crystallography (45), and metmyoglobin-Xe association constants have been measured to be approximately 200 and 10 M −1 (45,46). Comparable affinities have been determined for other naturally occurring sites in hemoglobin (44), lipoxygenase (47), and lipid transfer protein (48), as well as specially designed hydrophobic cavities in T4 lysozyme (49), ribose-binding protein (50), and other examples (51,52). We showed previously that xenon binds water-soluble cryptophanes approximately 1.5-fold less avidly in human plasma than in aqueous buffer solution (14).…”
Section: Resultsmentioning
confidence: 99%
“…Xenon binding to myoglobin has been well characterized by NMR spectroscopy (43,44) and X-ray crystallography (45), and metmyoglobin-Xe association constants have been measured to be approximately 200 and 10 M −1 (45,46). Comparable affinities have been determined for other naturally occurring sites in hemoglobin (44), lipoxygenase (47), and lipid transfer protein (48), as well as specially designed hydrophobic cavities in T4 lysozyme (49), ribose-binding protein (50), and other examples (51,52). We showed previously that xenon binds water-soluble cryptophanes approximately 1.5-fold less avidly in human plasma than in aqueous buffer solution (14).…”
Section: Resultsmentioning
confidence: 99%
“…[120] NMR of dissolved Xe has been applied to identify binding pockets of lipid transfer protein, [121] and for observation of conformational changes in maltose binding protein, [122] and chemotaxis Y protein. [123] Besides specific site affinity for native structures, protein engineering also allowed for the design of conformation-sensitive binding pockets as demonstrated with the ribose binding protein. [124] …”
Section: 129xe Cages and Hyper-cest Mrimentioning
confidence: 99%
“…In solution, 129 Xe can be used to probe protein structure 17-19 and physiologically important parameters such as blood oxygenation 20. Dissolved HP 129 Xe residing in the pulmonary capillaries rapidly diffuses into the alveolar gas spaces where its resonance frequency is shifted by ∼200 ppm.…”
Section: Introductionmentioning
confidence: 99%