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1H, 15N and13C resonance assignments of S2A mutant of human carbonic anhydrase II 人碳酸酐酶 II S2A 突变体的 1H、15N 和 13C 共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-03-23 DOI: 10.1007/s12104-024-10166-6
Neelam, Himanshu Singh

In preparation for a detailed exploration of the structural and functional aspects of the Ser2Ala mutant of human carbonic anhydrase II, we present here almost complete sequence-specific resonance assignments for 1H, 15N, and 13C. The mutation of serine to alanine at position 2, located in the N-terminal region of the enzyme, significantly alters the hydrophilic nature of the site, rendering it hydrophobic. Consequently, there is an underlying assumption that this mutation would repel water from the site. However, intriguingly, comparative analysis of the mutant structure with the wild type reveals minimal discernible differences. These assignments serve as the basis for in-depth studies on histidine dynamics, protonation states, and its intricate role in protein-water interactions and catalysis.

为了准备对人类碳酸酐酶 II 的 Ser2Ala 突变体的结构和功能方面进行详细的探索,我们在此提供了几乎完整的 1H、15N 和 13C 序列特异性共振赋值。位于酶 N 端区域的第 2 位丝氨酸突变为丙氨酸,大大改变了该位点的亲水性,使其成为疏水性位点。因此,有一种基本假设认为,这种突变会使该位点拒水。然而,有趣的是,对突变体结构与野生型结构的比较分析显示,两者之间的差异微乎其微。这些结果为深入研究组氨酸动力学、质子化状态及其在蛋白质与水的相互作用和催化作用中的复杂作用奠定了基础。
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引用次数: 0
Backbone 1H, 13C and 15N resonance assignment of the ubiquitin specific protease 7 catalytic domain (residues 208–554) in complex with a small molecule ligand 泛素特异性蛋白酶 7 催化结构域(残基 208-554)与小分子配体复合物的骨架 1H、13C 和 15N 共振赋值。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-03-12 DOI: 10.1007/s12104-024-10165-7
Maya J. Pandya, Wojciech Augustyniak, Matthew J. Cliff, Ilka Lindner, Anne Stinn, Jan Kahmann, Koen Temmerman, Hugh R. W. Dannatt, Jonathan P. Waltho, Martin J. Watson

The backbone 1H, 13C and 15N resonance assignment of Ubiquitin Specific Protease 7 catalytic domain (residues 208–554) was performed in its complex with a small molecule ligand and in its apo form as a reference. The amide 1H-15N signal intensities were boosted by an amide hydrogen exchange protocol, where expressed 2H, 13C, 15N-labeled protein was unfolded and re-folded to ensure exchange of amide deuterons to protons. The resonance assignments were used to determine chemical shift perturbations on ligand binding, which are consistent with the binding site observed by crystallography.

在泛素特异性蛋白酶 7 催化结构域(残基 208-554)与小分子配体的复合物中,以及作为参照物的apo形式中,对其进行了骨架 1H、13C 和 15N 共振赋值。通过酰胺氢交换方案提高了酰胺 1H-15N 信号强度,在该方案中,将表达的 2H、13C、15N 标记蛋白质展开并重新折叠,以确保酰胺氘核交换为质子。共振分配用于确定配体结合时的化学位移扰动,这与晶体学观察到的结合位点一致。
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引用次数: 0
Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2 人类 SERF2 的骨架 1H、13C 和 15N 化学位移分布图
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-03-11 DOI: 10.1007/s12104-024-10167-5
Bikash R. Sahoo, Vivekanandan Subramanian, James C.A. Bardwell

Human small EDRK-rich factor protein SERF2 is a cellular driver of protein amyloid formation, a process that has been linked to neurodegenerative diseases including Alzheimer’s and Parkinson’s disease. SERF2 is a 59 amino acid protein, highly charged, and well conserved whose structure and physiological function is unclear. SERF family proteins including human SERF2 have shown a tendency to form fuzzy complexes with misfolded proteins such as α-Synuclein which has been linked to Parkinson’s disease. SERF family proteins have been recently identified to bind nucleic acids, but the binding mechanism(s) remain enigmatic. Here, using multidimensional solution NMR, we report the 1H, 15N, and 13C chemical shift assignments (~ 86% of backbone resonance assignments) for human SERF2. TALOS-N predicted secondary structure of SERF2 showed three very short helices (3–4 residues long) in the N-terminal region of the protein and a long helix in the C-terminal region spanning residues 37–46 which is consistent with the helical content indicated by circular dichroism spectroscopy. Paramagnetic relaxation enhancement NMR analysis revealed that a short C-terminal region E53-K55 is in the proximity of the N-terminus. Having the backbone assignment of SERF2 allowed us to probe its interaction with α-Synuclein and to identify the residues in SERF2 binding interfaces that likely promote α-Synuclein aggregation.

人类富含 EDRK 的小因子蛋白 SERF2 是蛋白质淀粉样蛋白形成的细胞驱动因素,这一过程与包括阿尔茨海默氏症和帕金森氏症在内的神经退行性疾病有关。SERF2 是一种 59 个氨基酸的蛋白质,带高电荷,其结构和生理功能尚不清楚。包括人类 SERF2 在内的 SERF 家族蛋白显示出与折叠错误的蛋白质(如与帕金森病有关的 α-突触核蛋白)形成模糊复合物的倾向。最近发现 SERF 家族蛋白能与核酸结合,但其结合机制仍是个谜。在这里,我们利用多维溶液核磁共振,报告了人类 SERF2 的 1H、15N 和 13C 化学位移分配(约占骨干共振分配的 86%)。TALOS-N 预测的 SERF2 二级结构显示,该蛋白的 N 端区域有三个非常短的螺旋(3-4 个残基长),C 端区域有一个长螺旋,跨越 37-46 个残基,这与圆二色性光谱显示的螺旋含量一致。顺磁弛豫增强核磁共振分析表明,短 C 端区域 E53-K55 位于 N 端附近。有了 SERF2 的骨架分配,我们就能探究它与α-突触核蛋白的相互作用,并确定 SERF2 结合界面中可能促进α-突触核蛋白聚集的残基。
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引用次数: 0
NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4 来自动点核蛋白 KKT4 的 BRCT 结构域的核磁共振研究。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-03-07 DOI: 10.1007/s12104-024-10163-9
Patryk Ludzia, Hanako Hayashi, Timothy Robinson, Bungo Akiyoshi, Christina Redfield

KKT4 is a multi-domain kinetochore protein specific to kinetoplastids, such as Trypanosoma brucei. It lacks significant sequence similarity to known kinetochore proteins in other eukaryotes. Our recent X-ray structure of the C-terminal region of KKT4 shows that it has a tandem BRCT (BRCA1 C Terminus) domain fold with a sulfate ion bound in a typical binding site for a phosphorylated serine or threonine. Here we present the 1H, 13C and 15N resonance assignments for the BRCT domain of KKT4 (KKT4463–645) from T. brucei. We show that the BRCT domain can bind phosphate ions in solution using residues involved in sulfate ion binding in the X-ray structure. We have used these assignments to characterise the secondary structure and backbone dynamics of the BRCT domain in solution. Mutating the residues involved in phosphate ion binding in T. brucei KKT4 BRCT results in growth defects confirming the importance of the BRCT phosphopeptide-binding activity in vivo. These results may facilitate rational drug design efforts in the future to combat diseases caused by kinetoplastid parasites.

KKT4 是一种多域动核蛋白,专属于动核细胞,如布氏锥虫。它与其他真核生物的已知动核蛋白缺乏明显的序列相似性。我们最近对 KKT4 C 端区域的 X 射线结构显示,它有一个串联的 BRCT(BRCA1 C Terminus)结构域折叠,硫酸根离子与磷酸化丝氨酸或苏氨酸的典型结合位点结合。在这里,我们介绍了布鲁氏菌 KKT4(KKT4463-645)BRCT 结构域的 1H、13C 和 15N 共振分配。我们利用 X 射线结构中参与硫酸根离子结合的残基,证明 BRCT 结构域能在溶液中结合磷酸根离子。我们利用这些分配来描述 BRCT 结构域在溶液中的二级结构和骨架动力学特征。突变布鲁氏菌 KKT4 BRCT 中参与磷酸盐离子结合的残基会导致生长缺陷,这证实了 BRCT 磷肽结合活性在体内的重要性。这些结果可能有助于未来的合理药物设计工作,以防治由内生寄生虫引起的疾病。
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引用次数: 0
1H, 13C and 15N backbone resonance assignments of hepatocyte nuclear factor-1-beta (HNF1β) POUS and POUHD 肝细胞核因子-1-β(HNF1β)POUS 和 POUHD 的 1H、13C 和 15N 主干共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-03-07 DOI: 10.1007/s12104-024-10168-4
Sayaka Hokazono, Eri Imagawa, Daishi Hirano, Takahisa Ikegami, Kimihiko Oishi, Tsuyoshi Konuma

Hepatocyte nuclear factor 1β (HNF1β) is a transcription factor that plays a key role in the development and function of the liver, pancreas, and kidney. HNF1β plays a key role in early vertebrate development and the morphogenesis of these organs. In humans, heterozygous mutations in the HNF1B gene can result in organ dysplasia, making it the most common cause of developmental renal diseases, including renal cysts, renal malformations, and familial hypoplastic glomerular cystic kidney disease. Pathogenic variants in the HNF1B gene are known to cause various diseases, including maturity-onset diabetes of the young and developmental renal diseases. This study presents the backbone resonance assignments of HNF1β POUS and POUHD domains, which are highly conserved domains required for the recognition of double-stranded DNA. Our data will be useful for NMR studies to verify the altered structures and functions of mutant HNF1B proteins that can induce developmental renal diseases, including renal cysts, renal malformations, and familial hypoplastic glomerular cystic kidney disease. This study will provide the structural basis for future studies to elucidate the molecular mechanisms underlying how mutations in HNF1β cause diseases.

肝细胞核因子 1β(HNF1β)是一种转录因子,在肝脏、胰腺和肾脏的发育和功能中起着关键作用。HNF1β 在脊椎动物的早期发育和这些器官的形态发生中起着关键作用。在人类中,HNF1B 基因的杂合子突变可导致器官发育不良,是导致肾脏发育疾病(包括肾囊肿、肾畸形和家族性肾小球发育不全囊性肾病)的最常见原因。已知 HNF1B 基因的致病变异可导致多种疾病,包括成熟期发病的青年糖尿病和发育性肾病。本研究展示了 HNF1β POUS 和 POUHD 结构域的骨架共振分配,这两个结构域是识别双链 DNA 所需的高度保守结构域。我们的数据将有助于核磁共振研究验证突变型 HNF1B 蛋白结构和功能的改变,这些突变型 HNF1B 蛋白可诱发肾脏发育疾病,包括肾囊肿、肾畸形和家族性肾小球发育不全囊性肾病。这项研究将为今后的研究提供结构基础,以阐明 HNF1β 突变如何导致疾病的分子机制。
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引用次数: 0
Chemical shift assignments of the ACID domain of MED25, a subunit of the mediator complex in Arabidopsis thaliana 拟南芥介导复合体亚基 MED25 的 ACID 结构域的化学位移分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2024-02-09 DOI: 10.1007/s12104-024-10164-8
Yue Xiong, Jiang Zhu, Rui Hu, Ying Li, Yunhuang Yang, Maili Liu

Mediator complex is a key component that bridges various transcription activators and RNA polymerase during eukaryotic transcription initiation. The Arabidopsis thaliana Med25 (aMed25), a subunit of the Mediator complex, plays important roles in regulating hormone signaling, biotic and abiotic stress responses and plant development by interacting with a variety of transcription factors through its activator-interacting domain (ACID). However, the recognition mechanism of aMed25-ACID for various transcription factors remains unknown. Here, we report the nearly complete 1H, 13C, and 15N backbone and side chain resonance assignments of aMED25-ACID (residues 551–681). TALOS-N analysis revealed that aMED25-ACID structure is comprised of three α-helices and seven β-strands, which lacks the C-terminal α-helix existing in the human MED25-ACID. This study lays a foundation for further research on the structure-function relationship of aMED25-ACID.

介导复合体是真核生物转录起始过程中连接各种转录激活剂和 RNA 聚合酶的关键元件。拟南芥 Med25(aMed25)是 Mediator 复合物的一个亚基,通过其激活剂相互作用结构域(ACID)与多种转录因子相互作用,在调节激素信号转导、生物和非生物胁迫反应以及植物发育方面发挥着重要作用。然而,aMed25-ACID 与各种转录因子的识别机制仍然未知。在这里,我们报告了几乎完整的 aMED25-ACID(残基 551-681)的 1H、13C 和 15N 主干和侧链共振赋值。TALOS-N分析显示,aMED25-ACID结构由三个α螺旋和七个β链组成,缺少人MED25-ACID中存在的C端α螺旋。这项研究为进一步研究aMED25-ACID的结构与功能关系奠定了基础。
{"title":"Chemical shift assignments of the ACID domain of MED25, a subunit of the mediator complex in Arabidopsis thaliana","authors":"Yue Xiong,&nbsp;Jiang Zhu,&nbsp;Rui Hu,&nbsp;Ying Li,&nbsp;Yunhuang Yang,&nbsp;Maili Liu","doi":"10.1007/s12104-024-10164-8","DOIUrl":"10.1007/s12104-024-10164-8","url":null,"abstract":"<div><p>Mediator complex is a key component that bridges various transcription activators and RNA polymerase during eukaryotic transcription initiation. The <i>Arabidopsis thaliana</i> Med25 (aMed25), a subunit of the Mediator complex, plays important roles in regulating hormone signaling, biotic and abiotic stress responses and plant development by interacting with a variety of transcription factors through its activator-interacting domain (ACID). However, the recognition mechanism of aMed25-ACID for various transcription factors remains unknown. Here, we report the nearly complete <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone and side chain resonance assignments of aMED25-ACID (residues 551–681). TALOS-N analysis revealed that aMED25-ACID structure is comprised of three α-helices and seven β-strands, which lacks the C-terminal α-helix existing in the human MED25-ACID. This study lays a foundation for further research on the structure-function relationship of aMED25-ACID.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":null,"pages":null},"PeriodicalIF":0.8,"publicationDate":"2024-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139705700","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
NMR 1H, 13C, 15N backbone resonance assignments of wild-type human K-Ras and its oncogenic mutants G12D and G12C bound to GTP 野生型人K-Ras及其与GTP结合的致癌突变体G12D和G12C的NMR 1H、13C、15N骨架共振分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2023-11-10 DOI: 10.1007/s12104-023-10162-2
Chunhua Yuan, Alexandar L. Hansen, Lei Bruschweiler-Li, Rafael Brüschweiler

Human K-Ras protein, which is a member of the GTPase Ras family, hydrolyzes GTP to GDP and concomitantly converts from its active to its inactive state. It is a key oncoprotein, because several mutations, particularly those at residue position 12, occur with a high frequency in a wide range of human cancers. The K-Ras protein is therefore an important target for developing therapeutic anti-cancer agents. In this work we report the almost complete sequence-specific resonance assignments of wild-type and the oncogenic G12C and G12D mutants in the GTP-complexed active forms, including the functionally important Switch I and Switch II regions. These assignments serve as the basis for a comprehensive functional dynamics study of wild-type K-Ras and its G12 mutants.

人类K-Ras蛋白是GTP酶Ras家族的一员,它将GTP水解为GDP,并同时从活性状态转化为非活性状态。它是一种关键的癌蛋白,因为一些突变,特别是残基位置12的突变,在广泛的人类癌症中发生频率很高。因此,K-Ras蛋白是开发治疗性抗癌剂的重要靶点。在这项工作中,我们报道了GTP复合活性形式的野生型和致癌G12C和G12D突变体的几乎完整的序列特异性共振分配,包括功能重要的开关I和开关II区域。这些任务为野生型K-Ras及其G12突变体的全面功能动力学研究奠定了基础。
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引用次数: 0
13C and 15N resonance assignments of alpha synuclein fibrils amplified from Lewy Body Dementia tissue Lewy体痴呆组织中α-突触核蛋白原纤维的13C和15N共振定位
IF 0.9 4区 生物学 Q4 Biochemistry, Genetics and Molecular Biology Pub Date : 2023-11-03 DOI: 10.1007/s12104-023-10156-0
Alexander M. Barclay, Dhruva D. Dhavale, Collin G. Borcik, Moses H. Milchberg, Paul T. Kotzbauer, Chad M. Rienstra

Fibrils of the protein α-synuclein (Asyn) are implicated in the pathogenesis of Parkinson Disease, Lewy Body Dementia, and Multiple System Atrophy. Numerous forms of Asyn fibrils have been studied by solid-state NMR and resonance assignments have been reported. Here, we report a new set of 13C, 15N assignments that are unique to fibrils obtained by amplification from postmortem brain tissue of a patient diagnosed with Lewy Body Dementia.

α-突触核蛋白纤维蛋白(Asyn)与帕金森病、路易体痴呆和多系统萎缩的发病机制有关。已经通过固态NMR研究了多种形式的Asyn原纤维,并且已经报道了共振分配。在这里,我们报道了一组新的13C,15N分配,这是通过从一名被诊断为路易体痴呆的患者死后脑组织中扩增获得的原纤维所特有的。
{"title":"13C and 15N resonance assignments of alpha synuclein fibrils amplified from Lewy Body Dementia tissue","authors":"Alexander M. Barclay,&nbsp;Dhruva D. Dhavale,&nbsp;Collin G. Borcik,&nbsp;Moses H. Milchberg,&nbsp;Paul T. Kotzbauer,&nbsp;Chad M. Rienstra","doi":"10.1007/s12104-023-10156-0","DOIUrl":"10.1007/s12104-023-10156-0","url":null,"abstract":"<div><p>Fibrils of the protein α-synuclein (Asyn) are implicated in the pathogenesis of Parkinson Disease, Lewy Body Dementia, and Multiple System Atrophy. Numerous forms of Asyn fibrils have been studied by solid-state NMR and resonance assignments have been reported. Here, we report a new set of <sup>13</sup>C, <sup>15</sup>N assignments that are unique to fibrils obtained by amplification from postmortem brain tissue of a patient diagnosed with Lewy Body Dementia.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2023-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71908574","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM 金黄色葡萄球菌LytM催化结构域的化学位移分配。
IF 0.8 4区 生物学 Q4 BIOPHYSICS Pub Date : 2023-11-02 DOI: 10.1007/s12104-023-10161-3
Helena Tossavainen, Ilona Pitkänen, Lina Antenucci, Chandan Thapa, Perttu Permi

S. aureus resistance to antibiotics has increased rapidly. MRSA strains can simultaneously be resistant to many different classes of antibiotics, including the so-called “last-resort” drugs. Resistance complicates treatment, increases mortality and substantially increases the cost of treatment. The need for new drugs against (multi)resistant S. aureus is high. M23B family peptidoglycan hydrolases, enzymes that can kill S. aureus by cleaving glycine-glycine peptide bonds in S. aureus cell wall are attractive targets for drug development because of their binding specificity and lytic activity. M23B enzymes lysostaphin, LytU and LytM have closely similar catalytic domain structures. They however differ in their lytic activities, which can arise from non-conserved residues in the catalytic groove and surrounding loops or differences in dynamics. We report here the near complete 1H/13C/15N resonance assignment of the catalytic domain of LytM, residues 185–316. The chemical shift data allow comparative structural and functional studies between the enzymes and is essential for understanding how these hydrolases degrade the cell wall.

金黄色葡萄球菌对抗生素的耐药性迅速增加。耐甲氧西林金黄色葡萄球菌菌株可以同时对许多不同种类的抗生素产生耐药性,包括所谓的“最后手段”药物。耐药性使治疗复杂化,增加死亡率,并大大增加治疗成本。对抗(多重)耐药性金黄色葡萄球菌新药的需求很高。M23B家族肽聚糖水解酶是一种可以通过裂解金黄色葡萄球菌细胞壁中的甘氨酸-甘氨酸肽键来杀死金黄色葡萄菌的酶,由于其结合特异性和裂解活性,是药物开发的有吸引力的靶点。M23B酶溶酶体蛋白酶、LytU和LytM具有非常相似的催化结构域结构。然而,它们的裂解活性不同,这可能是由催化槽和周围环中的非保守残基或动力学差异引起的。我们在这里报道了LytM的催化结构域残基185-316的几乎完全的1H/13C/15N共振分配。化学位移数据允许对酶之间的结构和功能进行比较研究,对于了解这些水解酶如何降解细胞壁至关重要。
{"title":"Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM","authors":"Helena Tossavainen,&nbsp;Ilona Pitkänen,&nbsp;Lina Antenucci,&nbsp;Chandan Thapa,&nbsp;Perttu Permi","doi":"10.1007/s12104-023-10161-3","DOIUrl":"10.1007/s12104-023-10161-3","url":null,"abstract":"<div><p><i>S. aureus</i> resistance to antibiotics has increased rapidly. MRSA strains can simultaneously be resistant to many different classes of antibiotics, including the so-called “last-resort” drugs. Resistance complicates treatment, increases mortality and substantially increases the cost of treatment. The need for new drugs against (multi)resistant <i>S. aureus</i> is high. M23B family peptidoglycan hydrolases, enzymes that can kill <i>S. aureus</i> by cleaving glycine-glycine peptide bonds in <i>S. aureus</i> cell wall are attractive targets for drug development because of their binding specificity and lytic activity. M23B enzymes lysostaphin, LytU and LytM have closely similar catalytic domain structures. They however differ in their lytic activities, which can arise from non-conserved residues in the catalytic groove and surrounding loops or differences in dynamics. We report here the near complete <sup>1</sup>H/<sup>13</sup>C/<sup>15</sup>N resonance assignment of the catalytic domain of LytM, residues 185–316. The chemical shift data allow comparative structural and functional studies between the enzymes and is essential for understanding how these hydrolases degrade the cell wall.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":null,"pages":null},"PeriodicalIF":0.8,"publicationDate":"2023-11-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11082022/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71419439","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Correction to: NMR resonance assignments of 18.5 kDa complex of Arabidopsis thaliana DRB7.2:DRB4 interaction domains 更正:拟南芥DRB7.2的18.5kDa复合物的NMR共振分配:DRB4相互作用结构域。
IF 0.9 4区 生物学 Q4 Biochemistry, Genetics and Molecular Biology Pub Date : 2023-11-01 DOI: 10.1007/s12104-023-10152-4
Sneha Paturi, Mandar V. Deshmukh
{"title":"Correction to: NMR resonance assignments of 18.5 kDa complex of Arabidopsis thaliana DRB7.2:DRB4 interaction domains","authors":"Sneha Paturi,&nbsp;Mandar V. Deshmukh","doi":"10.1007/s12104-023-10152-4","DOIUrl":"10.1007/s12104-023-10152-4","url":null,"abstract":"","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2023-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71419440","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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Biomolecular NMR Assignments
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