Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism-Reference-Cited by-同舟云学术

Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism

Published:1996-06 Issue:3 Volume:1 Page:189-208
ISSN:1359-0278
Container-title:Folding and Design
language:en
Short-container-title:Folding and Design

Author:

Neira José L,Davis Ben,Ladurner Andreas G,Buckle Ashley M,de Prat Gay Gonzalo,Fersht Alan R

Publisher

Elsevier BV

Subject

Molecular Medicine,Biochemistry

Reference73 articles.

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3. Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals;Ludvigsen;J. Mol. Biol,1991

4. Comparison of the solution structure and X-ray structure of barley serine proteinase inhibitor 2;Clore;Protein Eng,1987

5. Crystal and molecular structure of the serine protease inhibitor (CI-2) from barley seeds;McPhalen;Biochemistry,1987

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