Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1973-9-4
pubmed:abstractText
Distinct structural regions have been found in several globular proteins composed of single polypeptide chains. The existence of such regions and the continuity of peptide chain within them, coupled with kinetic arguments, suggests that the early stages of three-dimensional structure formation (nucleation) occur independently in separate parts of these molecules. A nucleus can grow rapidly by adding peptide chain segments that are close to the nucleus in aminoacid sequence. Such a process would generate three-dimensional (native) protein structures that contain separate regions of continuous peptide chain. Possible means of testing this hypothesis are discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-13305131, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-14253427, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-14404936, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-15442905, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-16577722, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4343715, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4343716, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4501531, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4508127, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4508129, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4508131, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4508136, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4508154, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4638988, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4927987, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4956559, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4979054, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-4991411, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5014928, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5016646, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5069789, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5110314, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5261026, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5289387, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5460889, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5476919, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5484470, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5543977, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5551392, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5778276, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-5911639, http://linkedlifedata.com/resource/pubmed/commentcorrection/4351801-6043657
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Albumins, http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin, http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins, http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Malate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Muramidase, http://linkedlifedata.com/resource/pubmed/chemical/Myoglobin, http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase, http://linkedlifedata.com/resource/pubmed/chemical/Papain, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoglycerate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Rubredoxins, http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine, http://linkedlifedata.com/resource/pubmed/chemical/Subtilisins, http://linkedlifedata.com/resource/pubmed/chemical/Thermolysin, http://linkedlifedata.com/resource/pubmed/chemical/Trypsin, http://linkedlifedata.com/resource/pubmed/chemical/Trypsin Inhibitors
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
697-701
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:4351801-Albumins, pubmed-meshheading:4351801-Chymotrypsin, pubmed-meshheading:4351801-Immunoglobulins, pubmed-meshheading:4351801-L-Lactate Dehydrogenase, pubmed-meshheading:4351801-Malate Dehydrogenase, pubmed-meshheading:4351801-Models, Structural, pubmed-meshheading:4351801-Muramidase, pubmed-meshheading:4351801-Myoglobin, pubmed-meshheading:4351801-Pancreatic Elastase, pubmed-meshheading:4351801-Papain, pubmed-meshheading:4351801-Phosphoglycerate Kinase, pubmed-meshheading:4351801-Phosphoric Monoester Hydrolases, pubmed-meshheading:4351801-Protein Conformation, pubmed-meshheading:4351801-Ribonucleases, pubmed-meshheading:4351801-Rubredoxins, pubmed-meshheading:4351801-Serum Albumin, Bovine, pubmed-meshheading:4351801-Subtilisins, pubmed-meshheading:4351801-Thermolysin, pubmed-meshheading:4351801-Trypsin, pubmed-meshheading:4351801-Trypsin Inhibitors
pubmed:year
1973
pubmed:articleTitle
Nucleation, rapid folding, and globular intrachain regions in proteins.
pubmed:publicationType
Journal Article