W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick
{"title":"The following protein sequences were reprinted from the protein sequence database of the Protein Identification Resource (PIR).","authors":"W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Bair, D A Ferrick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 5","pages":"403-39"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13920692","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":"Examination of protein sequence homologies. VI. The evolution of Escherichia coli L7/L12 equivalent ribosomal proteins ('A' proteins), and the tertiary structure.","authors":"E Otaka, T Ooi, K Suzuki","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Sequence homologies among 23 complete and two partial sequences of ribosomal 'A' proteins from eukaryotes, metabacteria, eubacteria and chloroplasts, equivalent to Escherichia coli L7/L12, were examined using a correlation method that evaluates sequence similarity quantitatively. Examination of 325 comparison matrices prepared for possible combinations of the sequences indicates that 'A' protein sequences can be classified into two types: one is the \"prototype\" from eubacteria and chloroplasts, and the other is the \"transposition type\" from eukaryotes and metabacteria, which must have resulted from the internal transposition of the prototype sequence. The transposition type of eukaryotes can further be classified into P1 and P2 lines. Sequences of the P1 line are closer to those of metabacteria than to those of the P2 line. Eleven gaps, as deletion or insertion sites of amino acid residues, are necessary for an alignment of all the sequences. According to the crystallographic data for the C-terminal fragment (CTF) from E. coli L7, all the gaps involved in the CTF are located between segments that correspond to structural and functional elements such as alpha helix, beta strand, turning loop or hinge part. The existence of specific \"preservation units\" in these molecules is suggested. In contrast, the transposition site is located at the center of an alpha helix element that is involved in a folding domain, indicating that the transposition event was extremely drastic.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 5","pages":"395-402"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13816464","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":"Partial amino acid sequence of fructose-1,6-bisphosphatase from the blue-green algae Synechococcus leopoliensis.","authors":"F Marcus, S P Latshaw, M Steup, K P Gerbling","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Purified fructose-1,6-bisphosphatase from the cyanobacterium Synechococcus leopoliensis was S-carboxymethylated and cleaved with trypsin. The resulting peptides were purified by reversed-phase high performance liquid chromatography and the amino acid sequence of six of the purified peptides was determined by gas-phase microsequencing. The results revealed sequence homology with other fructose-1,6-bisphosphatases. The obtained sequence data provides information required for the design of oligonucleotide hybridization probes to screen existing libraries of cyanobacterial DNA. The determination of the amino acid sequence of cyanobacterial proteins may yield important information with respect to the endosymbiotic theory of evolution.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 5","pages":"391-3"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13695073","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}
A M Lesk, D R Boswell, V I Lesk, V E Lesk, A Bairoch
{"title":"A cross-reference table between the Protein Data Bank of macromolecular structures and the National Biomedical Research Foundation-Protein Identification Resource amino acid sequence data bank.","authors":"A M Lesk, D R Boswell, V I Lesk, V E Lesk, A Bairoch","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The National Biomedical Research Foundation-Protein Identification Resource (NBRF-PIR) and the Protein Data Bank at Brookhaven National Laboratory (PDB) both contain protein sequences. We have prepared a cross-reference index of the sequences in these data banks, and compared the data. Of the 270 cases of sequences of the same protein appearing in both data bases, for only 31% are the sequences identical. This is often the result of a difference in the state of maturation of the proteins rather than experimental error. Nevertheless is useful to be aware that the sequence information in these two data archives should not be regarded as redundant.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 4","pages":"295-308"},"PeriodicalIF":0.0,"publicationDate":"1989-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13910523","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":"Amino acid sequences of ferredoxins from rice cultivars, japonica and indica.","authors":"M Kamo, N Kotani, A Tsugita, Y K He, Y Nozu","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Ferredoxins were isolated from the leaves of two rice cultivars, japonica and indica. The purified protein preparations each contained two components, the major (I) and the minor (II) ferredoxin. Ferredoxin I from each cultivars was sequenced. The amino acid sequences of the ferredoxin I from the two strains were found to be identical to each other. The sequence similarity with wheat ferredoxin is about 90%. Most of the amino acid alterations are located at the ends of the protein, with the sequences surrounding the iron-sulfur coordinating cysteine residues being well conserved.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 4","pages":"289-93"},"PeriodicalIF":0.0,"publicationDate":"1989-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13910522","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}
W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Blair, D A Ferrick
{"title":"The following protein sequences were reprinted from the protein sequence database of the Protein Identification Resource (PIR).","authors":"W C Barker, L T Hunt, D G George, L S Yeh, H R Chen, M C Blomquist, E I Seibel-Ross, A Elzanowski, J K Blair, D A Ferrick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 4","pages":"309-83"},"PeriodicalIF":0.0,"publicationDate":"1989-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13910524","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}
Y Isashiki, T Noda, K Kobayashi, M Sase, T Saheki, K Titani
{"title":"Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase.","authors":"Y Isashiki, T Noda, K Kobayashi, M Sase, T Saheki, K Titani","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human argininosuccinate synthetase (ASS) activity was found to be inactivated by alpha-dicarbonyls such as 1,2-cyclohexanedione and phenylglyoxal in accordance with pseudo first-order kinetics. The enzyme was almost completely protected from this inactivation by Mg-ATP and partially by its analogues. The strongest protective effect against inactivation was found with Mg-ATP, followed by Mg-ADP, AMP, adenosine and Mg-inorganic pyrophosphate. These results suggest the importance of arginine residue(s) for Mg-ATP binding. We determined the amino acid sequence of the peptide with the highest specific radioactivity derived from ASS which had been labeled with [14C]phenylglyoxal and then cleaved by cyanogen bromide treatment. The sequence obtained, PEFYNRFKGRNDLM, corresponds to residues 148-161 of the amino acid sequence deduced from the cDNA nucleotide sequence determined by Bock et al. [Nucleic Acids Res 11:6505-6512, 1983], and has a high homology with the sequences of ATP-binding sites proposed for several ATP-requiring enzymes.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 4","pages":"283-7"},"PeriodicalIF":0.0,"publicationDate":"1989-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13927136","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":"Enzyme regions in structural and viral proteins.","authors":"P A Tsonis","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Enzyme sequences similar to structural and viral sequences are presented. Evolutionary and functional relationships are implicated from these findings.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 3","pages":"189-91"},"PeriodicalIF":0.0,"publicationDate":"1989-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13807344","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":"Inspection of three-dimensional structures of proteins with dynamical information from the normal mode analysis.","authors":"H Wako","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>In this paper it is demonstrated that, to analyze structural data of proteins obtained from X-ray crystallography, the normal mode analysis in dihedral angle space can serve to supplement X-ray data as a useful system for gaining information on their dynamical as well as static structures. Especially, the following two subjects are discussed; first, the breakdown of the motions of a limited region in a polypeptide chain (e.g., an alpha-helix, a beta-strand or a loop) into internal and external motions reveals whether the region is flexible, or it is rigid but mobile when it has large fluctuations. Second, the correlation map between atomic motions serves to provide information for dividing the chain into segments, such as domains or modules, from a dynamical rather than from a geometrical point of view. It is shown that the modules proposed by M. Go appear distinctly in the correlation map as the regions in which clusters of atoms with positive correlation coefficients of their movements to each other exist. Furthermore, the modules are characterized by the negative correlation coefficients of the movements of the atoms in the clusters in a particular module to such movements in a different module.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 3","pages":"175-80"},"PeriodicalIF":0.0,"publicationDate":"1989-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13894813","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}
G Brignon, M F Mahé, F Grosclaude, B Ribadeau-Dumas
{"title":"Sequence of caprine alpha s1-casein and characterization of those of its genetic variants which are synthesized at a high level, alpha s1-CnA, B and C.","authors":"G Brignon, M F Mahé, F Grosclaude, B Ribadeau-Dumas","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The sequence of caprine alpha s1-casein (199 residues) was established. The peptide chain has the same length as, and shows a 88% degree of identity with, its bovine counterpart. With the ovine alpha s1-casein, the sequence of which was deduced from that of its mRNA, the degree of identity is 97%, counting as one difference a deletion of eight residues in the ovine protein. The differences between the three genetic variants associated with a high alpha s1-casein content in milk are simple substitutions. Variant alpha s1-CnA differs from variant alpha s1-CnB by two substitutions, 16 Leu (A)----Pro (B) and 77 Gln (A)----Glu (B), the latter inducing the appearance of a phosphate group on 75 Ser. Variant alpha s1-CnC differs from alpha s1-CnB by three substitutions, 8 His (B)----Ile (C), 100 Arg (B)----Lys (C) and 195 Thr (B)----Ala (C). The original type of caprine alpha s1-casein could be another hypothetical genetic variant, having the same electrophoretic mobility as alpha s1-CnB.</p>","PeriodicalId":77336,"journal":{"name":"Protein sequences & data analysis","volume":"2 3","pages":"181-8"},"PeriodicalIF":0.0,"publicationDate":"1989-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13894814","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}