{"title":"Specificity of the amino acid content of endogenous regulatory oligopeptides.","authors":"A A Zamyatnin","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The amino acid residue content of endogenous regulatory oligopeptides possessing a certain spectrum of functional activity has been analyzed. It has been shown that compared to proteins, the oligopeptides contain a greater number of positively charged and cyclic radicals. All 579 oligopeptides contained in the EROP-Moscow data bank with the given spectrum of functional activity have been found to have common physicochemical characteristics.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"57-60"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13084242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Protein sequences and data analysis--new concept.","authors":"A Tsugita, H W Mewes, W C Barker","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"1"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13083478","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Turkey gizzard caldesmon: complete sequence of a C-terminal thrombic fragment that binds actin, tropomyosin and calmodulin.","authors":"J H Collins, J Leszyk, D Mornet, E Audemard","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We have determined, by protein chemistry methods, the complete amino acid sequence of a thrombic fragment, \"CaD35\", which contains the C-terminal 274 residues of turkey gizzard caldesmon. Residues 1-96 of CaD35 comprise an actin-binding subfragment which resembles the tropomyosin-binding segment of troponin T. Residues 111-128 and 255-272 may form basic, amphipathic helices that interact with calmodulin. Residues 251-253 (Ser-Ser-Ser) may be phosphorylated. Chymotryptic CaD35, obtained from chicken gizzard caldesmon, nearly identical in sequence to the turkey gizzard fragment, but contains an additional 32 amino acid residues at its N terminus.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"29-32"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13083481","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
C Caporale, L Carrano, G Nitti, E Poerio, P Pucci, V Buonocore
{"title":"Determination of the primary structure of an alpha-amylase inhibitor from wheat kernel by Edman degradation and fast atom bombardment mass spectrometry.","authors":"C Caporale, L Carrano, G Nitti, E Poerio, P Pucci, V Buonocore","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The primary structure of an alpha-amylase inhibitor (coded 0.39) from wheat kernel was determined by fast atom bombardment mass spectrometry and Edman degradation. The sequence is similar to an extent of 97% compared to the other major component of the monomeric isoinhibitor family coded 0.28. The differences consist of the substitution of a single residue and the deletion of two residues in inhibitor 0.39. Neither heterogeneity nor polymorphism were observed in the primary structures of the inhibitors.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"3-8"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12881749","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
B R Srinivasa, K R Swaminathan, C Ganapathy, R P Roy, S K Murthy, P J Vithayathil
{"title":"The primary structure of xylanase from Thermoascus aurantiacus.","authors":"B R Srinivasa, K R Swaminathan, C Ganapathy, R P Roy, S K Murthy, P J Vithayathil","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The amino acid sequence of xylanase isolated from the culture medium of Thermoascus aurantiacus was determined. It had 269 amino acid residues with an alpha-N-acetyl group at the amino terminus. The structure of blocked N-terminal 11 amino acid tryptic peptide except for acetylalanine was determined by sequence analysis of peptides derived from partial acid hydrolysis and from thermolysin digestion. The blocked N-terminal amino acid was determined as N-acetylalanine by electron ionization mass spectrometry. The sequence comparison of xylanase from T. aurantiacus with the xylanases of alkalophilic Bacillus sp C-125 and Cryptococcus albidus showed 40% similarity. Xylanase from T. aurantiacus had up to 15% similarity with the other two xylanases known. All the five xylanases showed a higher degree of similarity at the level of secondary structure.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"15-20"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13083479","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"EROP-Moscow: specialized data bank for endogenous regulatory oligopeptides.","authors":"A A Zamyatnin","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>At present we are familiar with several hundred endogenous oligopeptides involved in the functioning of the nervous, immune and endocrine systems. The information on their structures and functions is contained in a specially created data bank. Data on 865 regulatory oligopeptides with a total of 17,723 amino acid residues have been collected. Most molecules have about 10 amino acid residues, although the range chosen was from 2 to 50. The results obtained permitted us to define the difference between oligo- and polypeptides.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"49-52"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13083483","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Characterization of spinach ferredoxin-thioredoxin reductase.","authors":"A Tsugita, K Yano, L Gardet-Salvi, P Schürmann","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Ferredoxin-thioredoxin reductase (FTR) is an iron-sulfur protein which, in the presence of ferredoxin and thioredoxin, catalyses the activation of photosynthetic enzymes such as fructose-1,6-bisphosphatase, NADP-malate dehydrogenase and several others. The results from amino acid composition and N- and C-terminal sequences show that spinach FTR is composed of two nonidentical subunits (mol.wt. = 17,200: A; 15,500:B) present in equal amounts. Other components (mol. wt. = 16,300 and 14,200) observed in preparations are most likely derived from subunit A losing its amino terminal part. We report the amino acid compositions of the two subunits A and B of FTR including their partial terminal sequences. Subunit A has an additional amino-terminal serine-rich sequence which is phosphorylated.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"9-13"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13084244","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Principal component analysis to detect the similarity of distantly related proteins; its application to cytochromes c, c1 and f.","authors":"K Horimoto, H Suzuki, J Otsuka","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A new method has been developed for detecting the similarity between distantly related families of proteins. The amino acid sequences of each family of proteins are vertically aligned by a homologous alignment method and the physico-chemical properties of the amino acid residues at the corresponding site are evaluated simultaneously, by method of the principal component analysis. Taking into account the species diversity of each family of proteins, we assign the similar regions between the different families of proteins by the overlapping degree of the standard deviations around the mean values of the first principal component. To investigate the homologous relationship between the electron transport proteins in photosynthetic and O2 respiratory systems, this method has been applied to 70 species of mitochondrial cytochrome c, 4 species of cytochrome c1 and 7 species of cytochrome f. This analysis reveals that both cytochrome f and cytochrome c1 have large regions which are similar to those of cytochrome c. Assuming that these similar regions have the same stereochemical structures as those in cytochrome c, we can predict the outlines of the tertiary structures of cytochrome c1 and cytochrome f, respectively, each able to interact with its electron acceptor, cytochrome c and plastocyanin.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"33-42"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12821790","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The N-terminal amino acid sequence of phenol hydroxylase contains a dinucleotide-binding sequence motif.","authors":"T Sejlitz, C Wernstedt, U Hellman, H Y Neujahr","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The N-terminal sequence of phenol hydroxylase from Trichosporon cutaneum was determined by Edman degradation of the integral protein and of fragments obtained by hydroxylamine cleavage and by digestion with Staphylococcus V8 protease. A continuous sequence of 80 residues from the N terminus was determined: TKYSESYCDV10, LIVGAGPAGL20 MAARVLSEYV30 RQKPDLKVRI40 IDKRSTKVYN50 GQADGLQCRT60 LESLKNLRLA70 DKIXSEXNDM80. A single N-terminal sequence was detected, suggesting two identical subunits in the dimeric enzyme. We suggest the occurrence of an FAD-binding site near the N terminus. The C-terminal sequence is -LSTA, as determined by carboxypeptidase digestion.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"4 1","pages":"21-3"},"PeriodicalIF":0.0,"publicationDate":"1991-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13083480","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"N-terminal halves of gramicidin S synthetase 1, and tyrocidine synthetase 1 as novel members of firefly luciferase family.","authors":"H Toh","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>It was found, by computer-assisted homology search, that the N-terminal halves of gramicidin S synthetase 1 and tyrocidine synthetase 1 are homologous with beetle luciferases and plant 4-coumarate:CoA ligases. The comparison of the reactions catalyzed by these enzymes showed that they are involved in similar reactions; the adenylation of their substrates and the formation of thiolester. Structural and functional implication of the sequence homology and molecular evolution of these proteins are discussed.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"3 6","pages":"517-21"},"PeriodicalIF":0.0,"publicationDate":"1990-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13244802","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}