Biochimica et Biophysica Acta (BBA) - Protein Structure最新文献_第3页

Proton NMR investigation of Ln3+ complexes of thymopoietin32–36 胸腺生成素32 - 36 Ln3+配合物的质子核磁共振研究

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90093-3

Joseph B. Vaughn Jr. , Richard L. Stephens , Robert E. Lenkinski , N.Rama Krishna , George A. Heavner , Gideon Goldstein

{"title":"Proton NMR investigation of Ln3+ complexes of thymopoietin32–36","authors":"Joseph B. Vaughn Jr. , Richard L. Stephens , Robert E. Lenkinski , N.Rama Krishna , George A. Heavner , Gideon Goldstein","doi":"10.1016/0005-2795(81)90093-3","DOIUrl":"10.1016/0005-2795(81)90093-3","url":null,"abstract":"<div>The pentapeptide Arg-Lys-Asp-Val-Tyr (TP5) is a biologically active fragment of thymopoietin, the thymic hormone that induces selective T-cell differentiation. The formation of lanthanide(III) complexes of TP5 is demonstrated through the observation of Tb3+ fluorescence enhancement. The equilibria, stoichiometry and solution conformation of the La3+, Pr3+ and Yb3+ complexes of TP5 have been investigated using NMR spectroscopy. In addition, the dissociation constants of two methyl ester analogs of TP5 have been studied. Evidence is presented supporting an interaction between the arginine guanidino NϵH and the aspartate carboxylate of TP5. Binding of Ln3+ appears to be accompanied by a disruption (or weakening) of this interaction and a concomitant increase in the 180° rotamer population for the aspartate carboxylate group. The observed trends in the magnitudes of the dissociation constants and the rotamer populations appear to suggest that, although a significant amount of monodentate complexes may also exist, the metal ion binds predominantly to both carboxylates in a bidentate fashion.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90093-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18078144","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}

引用次数: 16

Characterization of C-reactive protein from the eggs of the marine teleost, cyclopterus lumpus L. 海洋硬骨鱼(cyclopterus lumpus L.)卵中c反应蛋白的表征。

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90092-1

Thelma C. Fletcher , Ann White , Arthur Youngson , Arpad Pusztai , Brian A. Baldo

引用次数: 10

Stability of lactate dehydrogenase 乳酸脱氢酶的稳定性

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90091-X

Joachim Müller, Cornelia Klein

{"title":"Stability of lactate dehydrogenase","authors":"Joachim Müller, Cornelia Klein","doi":"10.1016/0005-2795(81)90091-X","DOIUrl":"10.1016/0005-2795(81)90091-X","url":null,"abstract":"<div>Hybrids of lactate dehydrogenases from pig heart and muscle and from chicken heart and pig heart were obtained by the freeze-thaw method [1,2]. Ion-exchange chromatography of the resulting mixtures of hybrids yielded unusual elution patterns, i.e., the 2 + 2 hybrids (H2PM2P and H2CH2P) were eluted in two separate peaks. These subforms were concluded to result from partial resolution of the three geometric isomers. The hybrids of chicken heart and pig heart lactate dehydrogenase showed three distinct levels of stability. The characteristic temperatures of denaturation were 61.5°C for H4P, HCH3P and H2CH2PI; 71°C for H2CH2PII and H3CHP and 76.5°C for H4C. The resistance towards thermal denaturation thus seemed to be governed by the least stable dimer within the tetrameric enzyme. The arrangement of stabilities of the dimers was in excellent agreement with the number of additional ion pairs between Arg241 (chicken) and Asp57 (chicken and pig) [3] within the Q-contact areas. The rate-determining step of thermal denaturation of lactate dehydrogenase was concluded to comprise the distortion or dissociation of one of two Q-contacts of the tetramer.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90091-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18320413","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}

引用次数: 5

A novel protease may explain widely differing models for the structure of Artemia salina haemoglobin 一种新的蛋白酶可以解释盐蒿血红蛋白结构的广泛不同模型

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90100-8

Geoffrey W. Krissansen, Clive N.A. Trotman, Warren P. Tate

引用次数: 14

Inhibition of tubulin self-assembly in vitro by fluorodinitrobenzene 氟二硝基苯对体外微管蛋白自组装的抑制作用

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90095-7

Young C. Lee, Richard A. Yaple, Richard Baldridge, Mark Kirsch, Richard H. Himes

{"title":"Inhibition of tubulin self-assembly in vitro by fluorodinitrobenzene","authors":"Young C. Lee, Richard A. Yaple, Richard Baldridge, Mark Kirsch, Richard H. Himes","doi":"10.1016/0005-2795(81)90095-7","DOIUrl":"10.1016/0005-2795(81)90095-7","url":null,"abstract":"<div>The self-assembly of bovine brain tubulin into microtubules is inhibited by low molar ratios of 1-fluoro-2,4-dinitrobezene (FDNB). Binding studies using [14C]FDNB indicate that the incorporation of between one and two dinitrophenyl groups is sufficient to inhibit assembly completely, although more dinitrophenyl groups can be incorporated using higher FDNB/tubulin ratios. Dinitrophenyltubulin, under assembly conditions, tends to assemble into amorphous aggregates. Thiolysis by 2-mercaptoethanol removes the dinitrophenyl moieties. Paper chromatography and high-voltage electrophoresis of acid-hydrolyzed modified tubulin containing one dinitrophenyl group identified the residue as <math><mtext>S-</mtext><mtext>dinitrophenylcysteine</mtext></math>. The β-monomer of tubulin is preferentially modified at low FDNB/tubulin ratios. The reaction with FDNB is greatly reduced when tubulin is in polymerized form. FDNB reduces the colchicine binding activity but does not affect the Mg(II) content of the protein.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90095-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18320414","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}

引用次数: 21

Monte Carlo simulation study of thermal fluctuations and conformational energy surface of a small protein, basic pancreatic trypsin inhibitor 一种碱性胰蛋白酶抑制剂小蛋白表面热波动和构象能的蒙特卡罗模拟研究

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90098-2

Tosiyuki Noguti , Nobuhiro Gō , Tatsuo Ool , Ken Nishikawa

引用次数: 10

Crystalline actin tubes 晶体肌动蛋白管

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90089-1

Julian A. Barden, Paul M.G. Curmi, Cristobal G. Dos Remedios

{"title":"Crystalline actin tubes","authors":"Julian A. Barden, Paul M.G. Curmi, Cristobal G. Dos Remedios","doi":"10.1016/0005-2795(81)90089-1","DOIUrl":"10.1016/0005-2795(81)90089-1","url":null,"abstract":"<div>The effect of the trivalent cations scandium (Sc3+) and yttrium (Y3+) on the conformation of G-actin was examined using ultraviolet difference and high resolution 1H-NMR spectroscopy. A comparison was made with data obtained previously with the trivalent lanthanide cations (Ln3+). These results indicate that the first and subsequent Y ions (ionic radius 101.9 pm) behave exactly like Ln3+. Sc3+ is a smaller ion (87 pm) than any of the Ln3+. The first Sc3+ binds to a site on actin that is inaccessible to Mg2+, Y3+ and Ln3+. However, the second Sc3+ to bind behaves like an Ln3+. On replacing the native divalent cation (Mg2+), both Y3+ and Sc3+ mobilize the adenine ring of ATP bound to actin, thus exposing underlying residues to the solvent. When Y3+ and Sc3+ saturate their binding sites on actin, and when the ionic strength is raised to 0.1 M with KCI at pH 6.9, the actin aggregates. Y3+ binds to actin with a ratio of 6 : 1 and induces the aggregation of actin into crystalline actin tubes, whilstSc3+ Sc3+binds with a ratio of 8 : 1 and induces amorphous actin aggregates. These results are consistent with the suggestion that actin tubes are induced by trivalent cations, principally on the basis of their binding stoichiometry, which in turn is determined by ionic radius.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90089-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18320411","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}

引用次数: 8

The denatured states of cytochrome c 细胞色素c的变性状态

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90097-0

John P Harrington

{"title":"The denatured states of cytochrome c","authors":"John P Harrington","doi":"10.1016/0005-2795(81)90097-0","DOIUrl":"10.1016/0005-2795(81)90097-0","url":null,"abstract":"<div>The unfolding of horse ferricytochrome c in the presence of several inorganic salts has been studied under a variety of denaturing conditions and followed by means of absorbance changes in the Soret region (390–450 nm) and visible region (450–750 nm), as well as by viscosity measurements. Changes in the Soret region, usually sensitive to the heme environment, were characterized by gradual increases in absorbance at 409 nm for low concentrations of NaClO4 and LiClO4. As denaturant concentrations were increased, the low-spin state of the ferric heme is altered, as seen by a maximum shift to shorter wavelengths (402–407 nm) accompanied by a further increase in absorbance in the Soret region. Unlike the effect of several organic denaturants and the above salts, denaturation in the presence of LiCl and CaCl2 resulted in an overall decrease in the Soret region with a blue-shift to 401 and 400 nm, respectively. Visible spectra of ferricytochrome c exhibited new bands at 633 nm (9.0 M LiCl) and 636 nm (4.5 M CaCl2) indicative of a change in the spin state of the iron upon displacement of methionine 80. LiCl and LiBr produced intermediate states of protein unfolding with midpoints (<math><mtext>D</mtext><msub><mi></mi><mn><mtext>1</mtext><mtext>2</mtext></mn></msub></math>) at 4.0 and 8.6, and 2.6 and 6.4, respectively. A determination of ΔGUH2O and m, the free energy of unfolding in the absence of denaturant and the dependence of free energy of denaturation on denaturant concentration, was used to analyze the relative effectiveness of these denaturants.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90097-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17335886","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}

引用次数: 8

Spatial separation of the two essential thiol groups and the binding site of the exchangeable GTP in brain tubulin 脑小管蛋白中两个必需巯基的空间分离和可交换GTP的结合位点

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90086-6

Johanna Deinum , Margareta Wallin , Carl Lagercrantz

{"title":"Spatial separation of the two essential thiol groups and the binding site of the exchangeable GTP in brain tubulin","authors":"Johanna Deinum , Margareta Wallin , Carl Lagercrantz","doi":"10.1016/0005-2795(81)90086-6","DOIUrl":"10.1016/0005-2795(81)90086-6","url":null,"abstract":"<div>The assembly of microtubules from tubulin prepared without glycerol was inhibited by blocking the two most reactive sulfhydryl groups of the eight free sulfhydryl groups present per tubulin dimer. The assembly was also inhibited by Cu2+ ions in a redox-reaction with the two most reactive sulfhydryl groups. These two sulfhydryl groups had almost the same reactivity towards <math><mtext>N-</mtext><mtext>ethylmaleimide</mtext></math> and <math><mtext>p-</mtext><mtext>chloromercuribenzoate</mtext></math>, in spite of the fact that they are located on different subunits of tubulin. It was not possible to label just one single sulfhydryl group at a time by <math><mtext>N-</mtext><mtext>ethylmaleimide</mtext></math>, and it was not possible to decide whether one or two free sulfhydryl group(s) are needed for assembly. The EPR technique based on the interaction of spin labels with transition metals was used for the study of the distance between the two most reactive sulfhydryl groups and the sites of exchangeable GTP and Mg2+, respectively. The sulfhydryl groups were spin labelled with a nitroxide derivative of <math><mtext>N-</mtext><mtext>ethylmaleimide</mtext></math>. Cr(III)GTP was used as a paramagnetic substitute for GTP, and Mn2+ for Mg2+. It was found that: a. The exchange of GTP and the total content of GTP were not affected by modification of the sulfhydryl groups, b. The binding sites of the exchangeable GTP and Mg2+ are located 10 Å, at least, from the two most reactive sulfhydryl groups, c. The distance between the spin labels introduced on the two most reactive sulfhydryl groups was larger than 17 Å. The findings indicate that there is no direct interaction between exchangeable GTP and the two most reactive sulfhydryl groups.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90086-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17335885","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}

引用次数: 29

Primary structure of an acidic ribosomal protein YPA1 from Saccharomyces cerevisiae 酿酒酵母酸性核糖体蛋白YPA1的初级结构

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-11-30 DOI: 10.1016/0005-2795(81)90088-X

Takuzi Itoh

{"title":"Primary structure of an acidic ribosomal protein YPA1 from Saccharomyces cerevisiae","authors":"Takuzi Itoh","doi":"10.1016/0005-2795(81)90088-X","DOIUrl":"10.1016/0005-2795(81)90088-X","url":null,"abstract":"<div>The complete primary structure of an acidic ribosomal protein YPA1 from Saccharomyces cerevisiae has been determined. YPA1 is composed of 110 amino acid residues and has the composition: Asp7, Asn2, Thr2, Ser9, Glu15, Gln2, Pro3, Gly15, Ala21, Val6, Met2, Ile4, Leu9, Tyr2, Phe3, Lys7 and Arg1. The molecular weight of YPA1 is 11 020. The amino acid sequence was determined by <math><mtext>4-N,N-</mtext><mtext>dimethylaminoazobenzene</mtext></math> 4′-isothiocyanate degradation of the peptides obtained by digestions with trypsin, chymotrypsin, thermolysin, pepsin and Staphylococcus aureus protease of intact protein. A comparison of protein YPA1 from yeast with eL12 from Artemia salina shows a high sequence similarity. A considerable similarity is also shown with HL20 from Halobacterium cutirubrum. On the other hand, there is very little apparent sequence similarity between YPA1 and the eubacterial acidic protein L12 either from E. coli or B. subtilis.</div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90088-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18078143","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}

引用次数: 24