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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1997-4-10
|
| pubmed:abstractText |
Ribonuclease T1 can be unfolded and refolded without forming noticeable amounts of aggregates allowing to characterise the dimensions of a protein in different denatured states in terms of the Stokes radius RS. Upon thermal unfolding RS increases from 1.74 nm at 20 degrees C to 2.14 nm at 60 degrees C. By contrast, RS = 2.40 nm was obtained at 5.3 M guanidinium chloride (GuHCl) and 20 degrees C. Heating from 20 degrees C to 70 degrees C in the presence of 5.3 M GuHCl led to a 5% decrease in RS.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
403
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
245-8
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:9091310-Escherichia coli,
pubmed-meshheading:9091310-Guanidine,
pubmed-meshheading:9091310-Guanidines,
pubmed-meshheading:9091310-Hot Temperature,
pubmed-meshheading:9091310-Light,
pubmed-meshheading:9091310-Protein Denaturation,
pubmed-meshheading:9091310-Ribonuclease T1,
pubmed-meshheading:9091310-Scattering, Radiation
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Ribonuclease T1 has different dimensions in the thermally and chemically denatured states: a dynamic light scattering study.
|
| pubmed:affiliation |
Max-Delbrück-Center for Molecular Medicine Berlin-Buch, Germany. gast@orion.rz.mdc-berlin.de
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|