Linked Life Data

9367764

Source:http://linkedlifedata.com/resource/pubmed/id/9367764

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-12-5
pubmed:abstractText
Chymotrypsin inhibitor 2 (CI2) folds kinetically as a single domain protein. It has been shown that elements of native secondary structure do not significantly form in fragments as the 64 residue protein is progressively increased in length from its N terminus, until at least 60 residues are present. Here, we analyse peptides of increasing length from the C terminus and find that native-like structure is not present even in the largest, fragment (7-64). We have examined sets of peptides of the form (1 - x) and ((x + 1)-64) to detect complementation. The only pair that readily complements and gives native-like structure is (1-40) and (41-64), where cleavage occurs in the protease-binding loop of CI2. But, all the pairs of peptides (1 - x) + (41-64) complement for x > 40, as do all pairs of (1-40) + (x-64), where x < 40. The resultant complexes appear to be equivalent to (1-40). (41-64) with the overlapping sequence being unstructured. Thus, the folding of CI2 is extremely co-operative, and interactions have to be made between subdomains (1-40) and (41-64). This is consistent with the mechanism proposed for the folding pathway of intact CI2 in which a diffuse nucleus is formed in the transition state between the alpha-helix in the N-terminal region of the protein and conserved hydrophobic contacts in the C-terminal region of the polypeptide. It is with these protein design features that CI2 can be an effective protease inhibitor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
317-29
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9367764-Amino Acid Sequence, pubmed-meshheading:9367764-Anilino Naphthalenesulfonates, pubmed-meshheading:9367764-Circular Dichroism, pubmed-meshheading:9367764-Fluorescent Dyes, pubmed-meshheading:9367764-Guanidine, pubmed-meshheading:9367764-Kinetics, pubmed-meshheading:9367764-Magnetic Resonance Spectroscopy, pubmed-meshheading:9367764-Models, Molecular, pubmed-meshheading:9367764-Molecular Sequence Data, pubmed-meshheading:9367764-Peptide Fragments, pubmed-meshheading:9367764-Peptides, pubmed-meshheading:9367764-Plant Proteins, pubmed-meshheading:9367764-Protein Denaturation, pubmed-meshheading:9367764-Protein Folding, pubmed-meshheading:9367764-Protein Structure, Secondary, pubmed-meshheading:9367764-Serine Proteinase Inhibitors, pubmed-meshheading:9367764-Spectrometry, Fluorescence
pubmed:year
1997
pubmed:articleTitle
Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2.
pubmed:affiliation
MRC Cambridge Centre for Protein Engineering, MRC Centre, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't