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Literature DB >> 1422152

A refocused and optimized HNCA: increased sensitivity and resolution in large macromolecules.

B T Farmer¹, R A Venters, L D Spicer, M G Wittekind, L Müller.

Abstract

A 3D optimized, refocused HNCA experiment is described. It is demonstrated to yield a dramatic increase in sensitivity when applied to [13C, 15N]-labeled human carbonic anhydrase II, a 29-kDa protein. The reasons for the gain in sensitivity are discussed, and 3 distinct areas for further development are indicated.

Entities: Chemical Gene Species

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Year: 1992 PMID： 1422152 DOI： 10.1007/bf01875530

Source DB: PubMed Journal: J Biomol NMR ISSN： 0925-2738 Impact factor: 2.835

2 in total

1. An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins.

Authors: A Bax; M Ikura
Journal: J Biomol NMR Date: 1991-05 Impact factor: 2.835

2. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

Authors: M Ikura; L E Kay; A Bax
Journal: Biochemistry Date: 1990-05-15 Impact factor: 3.162

2 in total

26 in total

1. pK(a) values for the unfolded state under native conditions explain the pH-dependent stability of PGB1.

Authors: Stina Lindman; Mikael C Bauer; Mikael Lund; Carl Diehl; Frans A A Mulder; Mikael Akke; Sara Linse
Journal: Biophys J Date: 2010-11-17 Impact factor: 4.033

2. pH dependence of amide chemical shifts in natively disordered polypeptides detects medium-range interactions with ionizable residues.

Authors: Mario Pujato; Clay Bracken; Romina Mancusso; Marcela Cataldi; María Luisa Tasayco
Journal: Biophys J Date: 2005-08-19 Impact factor: 4.033

3. Covariance NMR in higher dimensions: application to 4D NOESY spectroscopy of proteins.

Authors: David A Snyder; Fengli Zhang; Rafael Brüschweiler
Journal: J Biomol NMR Date: 2007-09-18 Impact factor: 2.835

4. Interaction between p53 N terminus and core domain regulates specific and nonspecific DNA binding.

Authors: Fan He; Wade Borcherds; Tanjing Song; Xi Wei; Mousumi Das; Lihong Chen; Gary W Daughdrill; Jiandong Chen
Journal: Proc Natl Acad Sci U S A Date: 2019-04-15 Impact factor: 11.205

5. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.

Authors: Wade M Borcherds; Gary W Daughdrill
Journal: Methods Enzymol Date: 2018-10-22 Impact factor: 1.600

A refocused and optimized HNCA: increased sensitivity and resolution in large macromolecules.

1. An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins.

2. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

1. pK(a) values for the unfolded state under native conditions explain the pH-dependent stability of PGB1.

2. pH dependence of amide chemical shifts in natively disordered polypeptides detects medium-range interactions with ionizable residues.

3. Covariance NMR in higher dimensions: application to 4D NOESY spectroscopy of proteins.

4. Interaction between p53 N terminus and core domain regulates specific and nonspecific DNA binding.

5. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.

6. Minimisation of sensitivity losses due to the use of gradient pulses in triple-resonance NMR of proteins.

7. Determination of H(N),H (α) and H (N),C' coupling constants in (13)C, (15)N-labeled proteins.

Review 8. Resonance assignment strategies for the analysis of NMR spectra of proteins.

9. Backbone assignment, secondary structure and protein A binding of an isolated, human antibody VH domain.

10. 1H, 13C and 15N assignments and chemical shift-derived secondary structure of intestinal fatty acid-binding protein.