Linked Life Data

2023916

Source:http://linkedlifedata.com/resource/pubmed/id/2023916

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1991-5-31
pubmed:abstractText
Conformations of bovine pancreatic trypsin inhibitor were calculated by assuming that the final structure as well as properly chosen overlapping segments thereof are simultaneously in low-energy (not necessarily the lowest-energy) conformational states. Therefore, the whole chain can be built up from building blocks whose conformations are determined primarily by short-range interactions. Our earlier buildup procedure was modified by taking account of a statistical analysis of known amino acid sequences that indicates that there is nonrandom pairing of amino acid residues in short segments along the chain, and by carrying out energy minimization on only these segments and on the whole chain [without minimizing the energies of intermediate-size segments (20-30 residues long)]. Results of this statistical analysis were used to determine the variable sizes of the overlapping oligopeptide building blocks used in the calculations; these varied from tripeptides to octapeptides, depending on the amino acid sequence. Successive stages of approximations were used to combine the low-energy conformations of these building blocks in order to keep the number of variables in the computations to a manageable size. The calculations led to a limited number of conformations of the protein (only two different groups, with very similar structure within each group), most residues of which were in the same conformational state as in the native structure.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-1055397, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-1867723, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-2279846, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-2438420, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-2482758, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-2482759, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-2599756, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-3733319, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-3767948, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-4033149, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-4819639, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-6673746, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-6956920, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-839855, http://linkedlifedata.com/resource/pubmed/commentcorrection/2023916-875032
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3661-5
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Calculation of protein conformation as an assembly of stable overlapping segments: application to bovine pancreatic trypsin inhibitor.
pubmed:affiliation
Baker Laboratory of Chemistry, Cornell University, Ithaca, NY 14853-1301.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't