Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology最新文献

{"title":"Phosphorylation of the minimal inhibitory region at the C-terminus of caldesmon alters its structural and actin binding properties","authors":"Valerie B. Patchell ,&nbsp;Alexander V. Vorotnikov ,&nbsp;Yuan Gao ,&nbsp;Douglas G. Low ,&nbsp;James S. Evans ,&nbsp;Abdellatif Fattoum ,&nbsp;Mohammed El-Mezgueldi ,&nbsp;Steven B. Marston ,&nbsp;Barry A. Levine","doi":"10.1016/S0167-4838(02)00210-8","DOIUrl":"10.1016/S0167-4838(02)00210-8","url":null,"abstract":"<div><p>Caldesmon is an inhibitory protein believed to be involved in the regulation of thin filament activity in smooth muscles and is a major cytoplasmic substrate for MAP kinase. NMR spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750–779, alter upon MAP kinase phosphorylation of Ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to F-actin. The structural basis for the altered interaction is identified from the observation that phosphorylation destabilises a turn segment linking the two actin binding sites and thereby results in the randomisation of their relative disposition. This modulatory influence of Ser-759 phosphorylation is not merely a function of the bulkiness of the covalent modification since the stability of the turn region is observed to be sensitive to the ionisation state of the phosphate group. The data are discussed in the context of the inhibitory association of the C-terminal domain of caldesmon with F-actin.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00210-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84884196","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":"Legumain from bovine kidney: its purification, molecular cloning, immunohistochemical localization and degradation of annexin II and vitamin D-binding protein1","authors":"Takuya Yamane ,&nbsp;Keisuke Takeuchi ,&nbsp;Yoshio Yamamoto ,&nbsp;Yao-Hua Li ,&nbsp;Manabu Fujiwara ,&nbsp;Katuji Nishi ,&nbsp;Sho Takahashi ,&nbsp;Iwao Ohkubo","doi":"10.1016/S0167-4838(02)00209-1","DOIUrl":"https://doi.org/10.1016/S0167-4838(02)00209-1","url":null,"abstract":"<div><p>Legumain (asparaginyl endopeptidase) was purified to homogeneity from bovine kidneys. The molecular mass of the purified enzyme was calculated to be 34 000 by sodium dodecyl sulfate–polyacrylamide gel electrophoresis in the presence of β-mercaptoethanol. The enzyme rapidly hydrolyzed the substrate Z-Ala-Ala-Asn-MCA and was strongly inhibited by <em>N</em>-ethylmaleimide, <em>p</em>-chloromercuribenzene-sulfonic acid, Hg²⁺ and Cu²⁺. The amino acid sequence of the first 26 residues of the enzyme was Gly-Gly-Lys-His-Trp-Val-Val-Ile-Val-Ala-Gly-Ser-Asn-Gly-Gln-Tyr-Asn-Tyr-Arg-His-Gln-Ala-Phe-Ala-Asp-His-. This sequence is highly homologous to the sequences in the N-terminal of pig kidney legumain. We screened a bovine kidney cortex cDNA library using a DNA probe that originated from rat legumain, and we determined the bovine kidney cDNA structure and deduced the amino acid sequence. The cDNA is composed 1934 bp and encodes 433 amino acids in the coding region. The enzyme was strongly stained in the proximal tubules of the rat kidney in an immunohistochemical study. Vitamin D-binding protein which is known to be a ligand to megalin existing in the proximal tubules, was cleaved in a limited proteolytic manner by bovine kidney legumain. These results suggested that legumain contributes to the processing of macromolecules absorbed by proximal tubule cells. The enzyme also cleaved an N-terminal synthetic peptide of bovine annexin II (Gly²⁴-Ser-Val-Lys-Ala-Tyr-Thr³⁰-Asn-Phe-Asp-Ala-Glu³⁵-Arg-Asp³⁷) at a position between Asn³¹ and Phe³². The amino-terminal domain of annexin II has p11 subunit binding sites and phosphorylation sites for both pp60^src and protein kinase C. This suggests that legumain plays an important role in inactivation and degradation of annexin II, which is abundant in the receptor-recycling compartments of endosomes/lysosomes.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00209-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92085706","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":"Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data","authors":"Wayne W. Chan ,&nbsp;Steven L. Roderick ,&nbsp;David E. Cohen","doi":"10.1016/S0167-4838(01)00318-1","DOIUrl":"10.1016/S0167-4838(01)00318-1","url":null,"abstract":"<div><p>We have expressed, purified and crystallized recombinant human phosphatidylcholine transfer protein (PC-TP) and selenomethionyl PC-TP bound to dilinoleoyl phosphatidylcholine. The biochemical properties of native and selenomethionyl PC-TP were indistinguishable, and the two proteins crystallized under similar conditions. Both native and selenomethionyl PC-TP crystallized in two distinct space groups and diffracted X-rays to 2.4 Å resolution.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(01)00318-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79559738","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":"Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation","authors":"Richard T. Williams ,&nbsp;Paul V. Senior ,&nbsp;Leonie Van Stekelenburg ,&nbsp;Judith E. Layton ,&nbsp;Peter J. Smith ,&nbsp;Marie A. Dziadek","doi":"10.1016/S0167-4838(02)00211-X","DOIUrl":"10.1016/S0167-4838(02)00211-X","url":null,"abstract":"<div><p>Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions. A single sterile alpha motif (SAM) protein–protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins. We have defined the transmembrane topology of STIM1 by determining the sites of <em>N</em>-linked glycosylation. We have confirmed that STIM1 is modified by <em>N</em>-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen. Both <em>N</em>-linked oligosaccharides remain endoglycosidase H-sensitive, indicating absence of full processing within the ER and Golgi. This immature modification is nevertheless sufficient and critical for cell surface expression of STIM1. We show that STIM1–STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions. These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by <em>N</em>-linked glycosylation.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00211-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80832950","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":"Design of new and sensitive fluorogenic substrates for human kallikrein hK3 (prostate-specific antigen) derived from semenogelin sequences","authors":"Sophie Réhault ,&nbsp;Michèle Brillard-Bourdet ,&nbsp;Luc Bourgeois ,&nbsp;Gilles Frenette ,&nbsp;Luiz Juliano ,&nbsp;Francis Gauthier ,&nbsp;Thierry Moreau","doi":"10.1016/S0167-4838(02)00204-2","DOIUrl":"10.1016/S0167-4838(02)00204-2","url":null,"abstract":"<div><p>Human kallikrein hK3 (prostate-specific antigen) is a chymotrypsin-like serine protease which is widely used in the diagnosis of prostate cancer. Assays of the enzymatic activity of hK3 in extracellular fluids have been limited by a lack of sensitive synthetic substrates. This report describes the design of a series of internally quenched fluorescent peptides containing an amino acid sequence based on preferential hK3 cleavage sites in semenogelins. Those were identified by 2-D gel electrophoresis analysis and N-terminal sequencing of semenogelin fragments generated by ex vivo proteolysis in freshly ejaculated semen. These peptides were cleaved by hK3 at the C-terminal of certain tyrosyl or glutaminyl residues with <em>k</em>_cat/<em>K</em>_m values of 15 000–60 000 M⁻¹ s⁻¹. The substrate Abz-SSIYSQTEEQ-EDDnp was cleaved at the Tyr-Ser bond with a specificity constant <em>k</em>_cat/<em>K</em>_m of 60 000 M⁻¹ s⁻¹, making it the best substrate for hK3 described to date.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00204-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89625182","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":"Study of substrate–enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor","authors":"Chi-Chun Fong ,&nbsp;Wan-Ping Lai ,&nbsp;Yun-Chung Leung ,&nbsp;Samuel C.-L. Lo ,&nbsp;Man-Sau Wong ,&nbsp;Mengsu Yang","doi":"10.1016/S0167-4838(02)00208-X","DOIUrl":"10.1016/S0167-4838(02)00208-X","url":null,"abstract":"<div><p>Pyridoxal kinase (PK) is an important enzyme involved in bioactivation of vitamin B₆. Binding of PK with its substrate is the prerequisite step for the subsequent catalytic phosphorylation of the substrate. In the present study, a surface plasmon resonance biosensor (BIAcore) was employed to characterize the binding interaction between wild-type porcine PK and an immobilized substrate, pyridoxamine. Pyridoxamine was modified with 11-mercaptoundecanic acid and immobilized on a sensor chip through the formation of a self-assembled monolayer. The binding of PK to the immobilized pyridoxamine was followed in real time and the kinetic parameters were derived from non-linear analysis of the sensorgram. The effects of buffer pH, monovalent cations (Na⁺, K⁺) and divalent cations (Mn²⁺, Zn²⁺, Mg²⁺) on the binding kinetics were determined. Optimal pH for PK–pyridoxamine interaction in the absence of divalent ions is at around 7.4. While K⁺ increased and Na⁺ decreased the binding affinity (<em>K</em>_A) of PK to immobilized pyridoxamine, all divalent cations increased the <em>K</em>_A of PK for pyridoxamine. Solution phase affinity measurement based on a competitive binding assay was used to determine the affinities of PK for different vitamin B₆ analogues. The order of affinity of PK for different analogues is: pyridoxal-oxime&gt;pyridoxine&gt;pyridoxamine&gt;pyridoxal&gt;pyridoxal phosphate. This is the first study to demonstrate that buffer conditions such as pH and concentration of monovalent and/or divalent ions can directly alter the binding of PK for its substrates. The quantitative kinetic and thermodynamic parameters obtained by SPR measurement provide the insight information into the catalytic activity of this enzyme.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00208-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86491639","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":"Hydrolysis of pectins with different degrees and patterns of methylation by the endopolygalacturonase of Fusarium moniliforme","authors":"E. Bonnin ,&nbsp;A. Le Goff ,&nbsp;R. Körner ,&nbsp;J. Vigouroux ,&nbsp;P. Roepstorff ,&nbsp;J.-F. Thibault","doi":"10.1016/S0167-4838(02)00207-8","DOIUrl":"10.1016/S0167-4838(02)00207-8","url":null,"abstract":"<div><p>The mode of action of the endopolygalacturonase from <em>Fusarium moniliforme</em> was studied towards a series of pectins with different amounts and distribution patterns of methyl-ester groups. The enzyme hydrolysed the linkages between two galacturonic acid residues according to a multi-chain attack mechanism, at least at the early stage of the reaction. The final percentage of hydrolysis decreased with increasing the degree of methylation. The distribution pattern of the methyl groups affected the rate of hydrolysis as well as the final percentage of hydrolysis, a blockwise distribution being more favourable than a random one. The final products, as analysed by mass spectrometry, included methyl-esterified oligogalacturonates. The detailed analysis of the structure of the oligomers showed that the enzyme was able to accommodate methylated galacturonic acid in its active site, but that methyl-esterification negatively affected the affinity of the enzyme.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00207-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89796134","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":"Identifying sites of attachment of UV filters to proteins in older human lenses","authors":"J.A Aquilina,&nbsp;R.J.W Truscott","doi":"10.1016/S0167-4838(01)00313-2","DOIUrl":"10.1016/S0167-4838(01)00313-2","url":null,"abstract":"<div><p>Recent results indicate that covalent modification of proteins by tryptophan-derived UV filters may explain the age-dependent coloration of human lenses, and play a role in age-related cataract. The sites of attachment of the UV filters to the lens crystallins, however, have not been determined. This study utilized a database of predicted masses of UV filter-modified tryptic peptides to target sites of UV filter attachment. Proteins were isolated from old normal lenses and digested with trypsin at pH 6, in order to preserve the integrity of the sites of modification. Peptides were separated by high-performance liquid chromatography and characterized by mass spectrometry. Major colored and fluorescent peaks in the digest were found to correspond to cysteine-containing peptides in which the sulfur atom of the sidechain was linked to the major UV filter compound, 3-hydroxykynurenine glucoside. Three of the peptides originated from γS-crystallin and one from βB1-crystallin. These results show that a predicted mass database can be used to facilitate the identification of sites of UV filter modification in human lens crystallins. Furthermore, this work represents the first evidence that UV filters bind to specific residues on lens proteins in vivo, and suggests that sulfhydryl groups may be important sites for the attachment of UV filters.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(01)00313-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78447045","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":"Reaction of hydrogen peroxide and peroxidase activity in carboxymethylated cytochrome c: spectroscopic and kinetic studies","authors":"Swati Prasad ,&nbsp;Nakul C. Maiti ,&nbsp;Shyamalava Mazumdar ,&nbsp;Samaresh Mitra","doi":"10.1016/S0167-4838(02)00205-4","DOIUrl":"10.1016/S0167-4838(02)00205-4","url":null,"abstract":"<div><p>The peroxidase activity of carboxymethylated cytochrome <em>c</em> (Cmcytc) has been investigated by spectroscopic and kinetic techniques to examine the effect of carboxymethylation on the peroxidase activity of native cytochrome <em>c</em> (cytc). The optical spectrum suggests that the reaction of Cmcytc with H₂O₂ proceeds through only one intermediate, compound I. The apparent rate constant (<em>k</em>_app) for the reaction was found to be 17, 72 and 210 M⁻¹ s⁻¹ at pH 7.0, 5.0 and 3.5 respectively. These values are about 60 times larger than those reported for native cytc (0.236 M⁻¹ s⁻¹ at pH 7.0), and about five orders of magnitude lower than those for classical peroxidases. Cmcytc was found to catalyse oxidation of organic and inorganic substrates. The second order rate constant for the oxidation of 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) by Cmcytc (205 [H₂O₂] s⁻¹) is found to be larger than the corresponding value for native cytc (50 [H₂O₂] s⁻¹) at pH 6.0. The carboxymethylation of cytc ruptures the Fe-S (Met 80) bond and increases the rate of its reaction with H₂O₂, and its catalytic activity. The specific activity of Cmcytc was measured spectrophotometrically by the reported method using ABTS as substrate, and was found to be 288, 473 and 872 μM min⁻¹ mg⁻¹ at pH 7.0, 5.0 and 3.5 respectively. Resonance Raman studies indicated the presence of a bis-histidine coordinated form of Cmcytc at neutral pH, and the existence of a population distribution of different ligation states such as bis-histidine (HH), histidine-water (HW) and five coordinate (5C) forms at lower pH. The relative population of different species in Cmcytc was found to be HH (∼100%, ∼50%, ∼44%), HW (∼0%, ∼44%, 41%) and 5C (∼0%, ∼6%, 15%) at pH 7.0, 4.7 and 3.1 respectively. We have attempted to correlate the pH dependence of the reaction of Cmcytc with hydrogen peroxide and its peroxidase activity with the haem stereochemical structures observed for Cmcytc. Steady-state and time-resolved tryptophan fluorescence studies on Cmcytc were done to probe the conformational changes around the haem pocket of Cmcytc.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00205-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79849866","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":"Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D","authors":"Simon A. Cater ,&nbsp;Wendy E. Lees ,&nbsp;Jeffrey Hill ,&nbsp;Joze Brzin ,&nbsp;John Kay ,&nbsp;Lowri H. Phylip","doi":"10.1016/S0167-4838(02)00206-6","DOIUrl":"10.1016/S0167-4838(02)00206-6","url":null,"abstract":"<div><p>The interaction of a variety of aspartic proteinases with a recombinant tomato protein produced in <em>Pichia pastoris</em> was investigated. Only human cathepsin D and, even more potently, proteinase A from <em>Saccharomyces cerevisiae</em> were inhibited. The tomato polypeptide has &gt;80% sequence identity to a previously reported potato inhibitor of cathepsin D. Re-evaluation of the potato inhibitor revealed that it too was more potent (&gt;20-fold) towards yeast proteinase A than cathepsin D and so might be renamed the potato inhibitor of proteinase A. The potency towards yeast proteinase A may reflect a similarity between this fungal enzyme and aspartic proteinases produced by fungal pathogens which attack tomato and/or potatoes.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00206-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87507259","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}