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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4266
|
| pubmed:dateCreated |
1976-12-30
|
| pubmed:abstractText |
A new secondary structure, which shows regularity within the experimental error, is noticed in alpha-chymotrypsin, and considering its extended nature, the name epsilon-helix has been suggested for the same. The average observed values of phi and psi for this conformation are -93 degrees and +146 degrees, respectively. The helical parameters turn out to be n = 2.7 and h = 3.3 angstroms.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0036-8075
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
12
|
| pubmed:volume |
194
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
720-2
|
| pubmed:dateRevised |
2007-3-19
|
| pubmed:meshHeading | |
| pubmed:year |
1976
|
| pubmed:articleTitle |
Extended helical conformation newly observed in protein folding.
|
| pubmed:publicationType |
Journal Article
|