Linked Life Data

3553167

Source:http://linkedlifedata.com/resource/pubmed/id/3553167

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1987-5-26
pubmed:abstractText
Non-crystallographic approaches to the determination of protein structure must solve the problem of insufficient and low information content experimental data. Most successful methods augment experimentation with theoretical constraints (for example, potential energy functions or optimization error metrics). We believe it is important to separate the contributions of experimentation and theory in the construction of protein structure. The PROTEAN system defines protein topology on the basis of experimental data alone. Its performance on three data sets, derived from the lac-repressor headpiece of E. coli, sperm whale myoglobin, and domain 1 of bacteriophage T4 lysozyme, indicates that there may be families of related conformations that are consistent with the experimental data. These conformations provide insight into the strengths and weaknesses in the data sets. They also provide a set of structures with which to begin theoretical refinements. We outline here a strategy which maintains a clear distinction between refinements based on theory and those based on experiment, and thus allows a careful analysis of the properties of such refinement methods.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
100
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1403-23
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
New strategies for the determination of macromolecular structure in solution.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't