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Solution NMR studies of a 42 KDa Escherichia coli maltose binding protein/β-cyclodextrin complex: Chemical shift assignments and analysis
Kevin H. Gardner
Biophysics
Biophysics
Research output
:
Contribution to journal
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Article
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peer-review
135
Scopus citations
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Dive into the research topics of 'Solution NMR studies of a 42 KDa Escherichia coli maltose binding protein/β-cyclodextrin complex: Chemical shift assignments and analysis'. Together they form a unique fingerprint.
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Engineering & Materials Science
Maltose
100%
Chemical shift
93%
Cyclodextrins
92%
Carrier Proteins
88%
Escherichia coli
69%
Nuclear magnetic resonance
66%
Labeling
53%
Proteins
50%
Protonation
25%
Crystal structure
17%
Protons
16%
Electronic data interchange
14%
Carbon
10%
Experiments
4%
Medicine & Life Sciences
Maltose-Binding Proteins
80%
Cyclodextrins
75%
Escherichia coli Proteins
66%
Proteins
20%
Protons
14%
Carbon
13%
Chemical Compounds
Solution NMR
67%
Chemical Shift
44%
Val-Ile
36%
Val-Leu
34%
Protein
22%
Secondary Structure
19%
Methyl Group
9%
Proton
7%
Crystal Structure
5%
Carbon Atom
5%