chymotrypsin inhibitor 2

64 amino acids; partial amino acid sequence given in first source

Also Known As:

CH-IN-CI-2 protein, Hordeum vulgare; chymotrypsin inhibitor CI-2 (barley); chymotrypsin inhibitor CI-2 protein, Hordeum vulgare

Networked: 4 relevant articles (0 outcomes, 1 trials/studies)

Bio-Agent Context: Research Results

Amino Acids, Peptides, and Proteins: 1
- Proteins: 484843
  - Plant Proteins: 334
    - chymotrypsin inhibitor 2: 4
- Peptides: 82426
  - chymotrypsin inhibitor 2: 4

Experts

1.	Lu, Zhongyi: 1 article (06/2017)
2.	Wang, Yu: 1 article (06/2017)
3.	Xu, Feng: 1 article (06/2017)
4.	Zhu, Yudi: 1 article (06/2017)
5.	Zhu, Yuxi: 1 article (06/2017)
6.	Guth, Ulrich: 1 article (03/2008)
7.	Nölting, Bengt: 1 article (03/2008)
8.	Salimi, Neema: 1 article (03/2008)
9.	Andert, K: 1 article (11/2000)
10.	Nölting, B: 1 article (11/2000)

Related Diseases

1.	AIDS-Related Complex (ARC) 08/01/1998 - "Experimental and theoretical studies on the folding of small proteins such as the chymotrypsin inhibitor 2 (CI-2) and the P22 Arc repressor suggest that the folding transition state is an expanded version of the native state with most interactions partially formed. " 11/15/2000 - "The high structural resolution of the main transition states for the formation of native structure for the six small proteins of which Phi-values for a large set of mutants have become available, barstar, barnase, chymotrypsin inhibitor 2, Arc repressor, the src SH3 domain, and a tetrameric p53 domain reveals that for the first 5 of these proteins: (1) Residues that belong to regular secondary structure have a significantly larger average fraction of native structural consolidation than residues in loops; (2) on the other hand, secondary and tertiary structures have built up to the same degree, or at least a high degree, but nonuniformly distributed over the molecule; (3) the most consolidated parts of each protein molecule in the transition state cluster together, and these clusters contain a significantly higher percentage of residues that belong to regular secondary structure than the rest of the molecule. " 03/21/2008 - "We investigate the average inter-residue folding forces derived from mutational data of the 15 proteins: barstar, barnase, chymotrypsin inhibitor 2 (CI2), Src SH3 domain, spectrin R16 domain, Arc repressor, apo-azurin, cold shock protein B (cspB), C-terminal domain of ribosomal protein L9 (CTL9), FKBP12, alpha-lactalbumin, colicin E7 immunity protein 7 (IM7), colicin E9 immunity protein 9 (IM9), spectrin R17 domain, and ubiquitin. "
2.	Hyperoxia 06/01/2017 - "Newborn Sprague-Dawley rats were randomly divided in the newborn air group, newborn hyperoxia group and newborn intervention group, the latter of which was administered the chymotrypsin inhibitor, 2-(5-formylamino-6-oxo-2-phenyl-1, 6-dihydropyrimidine-1-yl)-N-[4-dioxo-1-phenyl-7-(2-pyridyloxy)] 2-heptyl-acetamide (NK3201). "

Related Drugs and Biologics

1.	Proteins (Proteins, Gene)
2.	Bacillus amyloliquefaciens barstar protein (barstar)
3.	Bacillus amyloliquefaciens ribonuclease
4.	Cold Shock Proteins and Peptides
5.	Ubiquitin
6.	Tacrolimus Binding Protein 1A (FKBP12)
7.	Spectrin
8.	Lactalbumin (alpha-Lactalbumin)
9.	Colicins
10.	Azurin