Identification of Residues Involved in the Interaction ofStaphylococcus aureusFibronectin-Binding Protein with the4F15F1 Module Pair of Human Fibronectin Using Heteronuclear NMR Spectroscopy†

Christopher J. Penkett; Christopher M. Dobson; Lorna J. Smith; Jeremy R. Bright; Andrew R. Pickford; Iain D. Campbell; Jennifer R. Potts

doi:10.1021/bi992267k

Identification of Residues Involved in the Interaction ofStaphylococcus aureusFibronectin-Binding Protein with the4F15F1 Module Pair of Human Fibronectin Using Heteronuclear NMR Spectroscopy†

Biochemistry ◽

10.1021/bi992267k ◽

2000 ◽

Vol 39 (11) ◽

pp. 2887-2893 ◽

Cited By ~ 18

Author(s):

Christopher J. Penkett ◽

Christopher M. Dobson ◽

Lorna J. Smith ◽

Jeremy R. Bright ◽

Andrew R. Pickford ◽

...

Keyword(s):

Nmr Spectroscopy ◽

Heteronuclear Nmr ◽

Binding Protein ◽

Heteronuclear Nmr Spectroscopy ◽

Human Fibronectin

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Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy

European Journal of Biochemistry ◽

10.1046/j.1432-1327.1998.2510781.x ◽

1998 ◽

Vol 251 (3) ◽

pp. 781-786 ◽

Cited By ~ 13

Author(s):

Azita Mesgarzadeh ◽

Stefania Pfeiffer ◽

Jan Engelke ◽

Dirck Lassen ◽

Heinz Ruterjans

Keyword(s):

Fatty Acid ◽

Nmr Spectroscopy ◽

Fatty Acid Binding Protein ◽

Heteronuclear Nmr ◽

Binding Protein ◽

Bound Water ◽

Fatty Acid Binding ◽

Acid Binding Protein ◽

Bovine Heart ◽

Heteronuclear Nmr Spectroscopy

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Unusual Helix-Containing Greek Keys in Development-Specific Ca2+-Binding Protein S. 1H, 15N, and 13C Assignments and Secondary Structure Determined with the Use of Multidimensional Double and Triple Resonance Heteronuclear NMR Spectroscopy

Biochemistry ◽

10.1021/bi00175a009 ◽

1994 ◽

Vol 33 (9) ◽

pp. 2409-2421 ◽

Cited By ~ 13

Author(s):

Stefan Bagby ◽

Timothy S. Harvey ◽

Lewis E. Kay ◽

Susan G. Eagle ◽

Sumiko Inouye ◽

...

Keyword(s):

Nmr Spectroscopy ◽

Secondary Structure ◽

Heteronuclear Nmr ◽

Binding Protein ◽

Protein S ◽

Triple Resonance ◽

Heteronuclear Nmr Spectroscopy

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Determination of the secondary structure of the DNA binding protein Ner from phage .mu. using proton homonuclear and nitrogen-15-proton heteronuclear NMR spectroscopy

Biochemistry ◽

10.1021/bi00438a027 ◽

1989 ◽

Vol 28 (12) ◽

pp. 5081-5089 ◽

Cited By ~ 29

Author(s):

Angela M. Gronenborn ◽

Paul T. Wingfield ◽

G. Marius Clore

Keyword(s):

Nmr Spectroscopy ◽

Secondary Structure ◽

Dna Binding ◽

Heteronuclear Nmr ◽

Binding Protein ◽

Dna Binding Protein ◽

Phage Mu ◽

Heteronuclear Nmr Spectroscopy

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Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.89.24.11673 ◽

1992 ◽

Vol 89 (24) ◽

pp. 11673-11677 ◽

Cited By ~ 20

Author(s):

M. Overduin ◽

B. Mayer ◽

C. B. Rios ◽

D. Baltimore ◽

D. Cowburn

Keyword(s):

Nmr Spectroscopy ◽

Secondary Structure ◽

Heteronuclear Nmr ◽

Src Homology 2 ◽

Heteronuclear Nmr Spectroscopy ◽

Src Homology ◽

Src Homology 2 Domain

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4-Oxalocrotonate tautomerase, a 41-kDa homohexamer: Backbone and side-chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy

Protein Science ◽

10.1002/pro.5560050418 ◽

1996 ◽

Vol 5 (4) ◽

pp. 729-741 ◽

Cited By ~ 13

Author(s):

James T. Stivers ◽

Chitrananda Abeygunawardana ◽

Christian P. Whitman ◽

Albert S. Mildvan

Keyword(s):

Nmr Spectroscopy ◽

Secondary Structure ◽

Active Site ◽

Heteronuclear Nmr ◽

Resonance Assignments ◽

Side Chain ◽

Active Site Residues ◽

Chain Resonance ◽

Heteronuclear Nmr Spectroscopy ◽

Side Chain Resonance

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Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy

Protein Science ◽

10.1002/pro.5560041218 ◽

1995 ◽

Vol 4 (12) ◽

pp. 2605-2615 ◽

Cited By ~ 81

Author(s):

M. Kirsten Frank ◽

G. Marius Clore ◽

Angela M. Gronenborn

Keyword(s):

Nmr Spectroscopy ◽

Heteronuclear Nmr ◽

Binding Domain ◽

Protein G ◽

Dynamic Characterization ◽

Denatured State ◽

Heteronuclear Nmr Spectroscopy ◽

Streptococcal Protein G ◽

Immunoglobulin Binding

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Application of Heteronuclear NMR Spectroscopy to Bioinorganic and Medicinal Chemistry ☆

Reference Module in Chemistry, Molecular Sciences and Chemical Engineering ◽

10.1016/b978-0-12-409547-2.10947-3 ◽

2018 ◽

Author(s):

Eirini Fotopoulou ◽

Luca Ronconi

Keyword(s):

Nmr Spectroscopy ◽

Medicinal Chemistry ◽

Heteronuclear Nmr ◽

Heteronuclear Nmr Spectroscopy

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Heteronuclear NMR spectroscopy of proteins encapsulated in cubic phase lipids

Journal of Magnetic Resonance ◽

10.1016/j.jmr.2019.06.017 ◽

2019 ◽

Vol 305 ◽

pp. 146-151 ◽

Cited By ~ 4

Author(s):

Thomas G. Meikle ◽

Ashish Sethi ◽

David W. Keizer ◽

Jeffrey J. Babon ◽

Frances Separovic ◽

...

Keyword(s):

Nmr Spectroscopy ◽

Heteronuclear Nmr ◽

Cubic Phase ◽

Heteronuclear Nmr Spectroscopy

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Three-dimensional structure of (1-71)bacterioopsin solubilized in methanol/chloroform and SDS micelles determined by 15N-1H heteronuclear NMR spectroscopy

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1994.tb19973.x ◽

1994 ◽

Vol 219 (1-2) ◽

pp. 571-583 ◽

Cited By ~ 71

Author(s):

Konstantine V. PERVUSHIN ◽

Vladislav Yu. OREKHOV ◽

Alexander I. POPOV ◽

Larisa Yu. MUSINA ◽

Alexander S. ARSENIEV

Keyword(s):

Nmr Spectroscopy ◽

Heteronuclear Nmr ◽

Three Dimensional ◽

Dimensional Structure ◽

Three Dimensional Structure ◽

Sds Micelles ◽

Heteronuclear Nmr Spectroscopy

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Heteronuclear NMR Spectroscopy of Lignins

Lignin and Lignans ◽

10.1201/ebk1574444865-c6 ◽

2010 ◽

pp. 245-265 ◽

Cited By ~ 15

Author(s):

Dimitris Argyropoulos

Keyword(s):

Nmr Spectroscopy ◽

Heteronuclear Nmr ◽

Heteronuclear Nmr Spectroscopy

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