α-Proton chemical shifts and secondary structure in proteins

Keywords

Chemical shift, Random coil, Chemistry, Amino acid residue, Protein secondary structure

References

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Cited by

• Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.Lawrence P. McIntosh, A. Joshua Wand, David F. Lowry — 1990
• High pressure NMR study of a small protein, gurmarinKyoko Inoue, Hiroaki Yamada, Toshiaki Imoto — 1998
• Pressure-dependent changes in the structure of the melittin α-helix determined by NMRMitsuo Iwadate, Tetsuo Asakura, Peter V. Dubovskii — 2001
• Structure and function of a pepstatin-insensitive acid proteinase from Aspergillus niger var. Macrosporus.Kenji Takahashi, Masaru Tanokura, Hideshi Inoue — 1991
• Chemical shifts as a tool for structure determination.David S. Wishart, Brian D. Sykes — 1994
• Periodic properties of proton conformational shifts in isolated protein helices. An experimental study.M. Ángeles Jiménez, Francisco J. Blanco, Manuel Rico — 1992
• Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRViewStephan Schwarzinger, Gerard Kroon, Ted R. Foss — 2000
• NMR assignments and secondary structure of the retinoid X receptor alpha DNA-binding domain. Evidence for the novel C-terminal helix.Min S. Lee, Daniel S. Sem, Steven A. Kliewer — 1994
• Molecular basis for co-operativity in Ca2+ binding to calbindin D9k. 1H nuclear magnetic resonance studies of (Cd2+)1-bovine calbindin D9k.Mikael Akke, Sture Forsén, Walter J. Chazin — 1991
• Kringle-2 domain of the tissue-type plasminogen activator. 1H-NMR assignments and secondary structure.In‐Ja L. Byeon, Robert F. Kelley, Miguel Llinás — 1991
• Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins.David A. Case, H. Jane Dyson, Peter E. Wright — 1994
• Nuclear Magnetic Resonance Spectroscopic Studies of Human Immunoglobulin ‘G’ in Alzheimer’s DiseaseSanjeev Mittal, Shweta Chaudhary — 2014
• Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor.Carlo P. M. van Mierlo, Nigel J. Darby, David Neuhaus — 1991
• Does the solid‐state structure of endothelin‐1 provide insights concerning the solution‐state conformational equilibrium?Gregory M. Lee, Chinpan Chen, T. Marschner — 1994
• Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopyDavid S. Wishart, Brian D. Sykes, F.M. Richards — 1991
• Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.C.H. Arrowsmith, Ruth Pachter, Russ B. Altman — 1990
• HIV-1 encoded virus protein U (Vpu) solution structure of the 41-62 hydrophilic region containing the phosphorylated sites Ser52 and Ser56.Gaël Coadou, Nathalie Evrard‐Todeschi, Josyane Gharbi‐Benarous — 2002
• A series of point mutations reveal interactions between the calcium‐binding sites of calmodulinMelissa A. Starovasnik, Rachel E. Klevit, Dai‐Rong Su — 1992
• The relationship between amide proton chemical shifts and secondary structure in proteinsTetsuo Asakura, Kazuhiro Taoka, Makoto Demura — 1995
• Analysis of proton chemical shifts in regular secondary structure of proteinsKlara �sapay, DavidA. Case — 1994

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