1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase and preliminary features of the structure in solution

Author:

Prompers Jeanine J.,Hilbers Cornelis W.,Groenewegen Anneke,Schaik René C. Van,Pepermans Henri A. M.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference65 articles.

1. Primary structure effects on peptide group hydrogen exchange;Bai;Proteins Struct Funct Genet,1993

2. Experimental NMR techniques for studies of biopolymers;Bax;Curr Opin Struct Biol,1991

3. 1H-1H correlation via isotropic mixing of 13C magnetization, a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins;Bax;J Magn Reson,1990a

4. Methodological advances in protein NMR;Bax;Acc Chem Res,1993

5. An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the α-carbon of the preceding residue in uniformly 15N/13C enriched proteins;Bax;J Biomol NMR,1991

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