1cis
CONTEXT DEPENDENCE OF PROTEIN SECONDARY STRUCTURE FORMATION. THE THREE-DIMENSIONAL STRUCTURE AND STABILITY OF A HYBRID BETWEEN CHYMOTRYPSIN INHIBITOR 2 AND HELIX E FROM SUBTILISIN CARLSBERGCONTEXT DEPENDENCE OF PROTEIN SECONDARY STRUCTURE FORMATION. THE THREE-DIMENSIONAL STRUCTURE AND STABILITY OF A HYBRID BETWEEN CHYMOTRYPSIN INHIBITOR 2 AND HELIX E FROM SUBTILISIN CARLSBERG
About this StructureAbout this Structure
1cis is a 1 chain structure with sequence from Hordeum vulgare. Full experimental information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Osmark P, Sorensen P, Poulsen FM. Context dependence of protein secondary structure formation: the three-dimensional structure and stability of a hybrid between chymotrypsin inhibitor 2 and helix E from subtilisin Carlsberg. Biochemistry. 1993 Oct 19;32(41):11007-14. PMID:8218165
- ↑ Huang JT, Tian J. Amino acid sequence predicts folding rate for middle-size two-state proteins. Proteins. 2006 May 15;63(3):551-4. PMID:16477599 doi:10.1002/prot.20911