Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals

Author:

Ludvigsen Svend,Shen Hengyi,Kjær Mogens,Madsen Jens Chr.,Poulsen Flemming M.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference25 articles.

1. Comparisons of the high resolution structures of the α-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals;Billeter;J. Mol. Biol.,1989

2. X-PLOR SOFTWARE;Brünger,1988

3. Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints; application to crambin;Brünger,1986

4. Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics;Clore;J. Mol. Biol.,1985

5. Application of molecular dynamics with interproton distance restraint to three-dimensional protein structure determination. A model study of crambin;Clore;J. Mol. Biol.,1986

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