High-resolution X-ray structure of the DNA-binding protein HU from the hyper-thermophilic Thermotoga maritima and the determinants of its thermostability View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-04

AUTHORS

Evangelos Christodoulou, Wojciech R. Rypniewski, Constantinos E. Vorgias

ABSTRACT

The histone-like DNA-binding proteins (HU) are a convenient model for studying factors affecting thermostability because of their relatively simple, easily comparable structures, their common function, and their presence in organisms of widely differing thermostability. We report the determination of the high-resolution structure (1.53 A) at 273 K and 100 K of the HU protein from the hyper-thermophilic eubacterium Thermotoga maritima(HU Tmar, T(m)=80.5 degrees C). The structural data presented clearly show that the HU Tmar has a fold similar to its thermophilic homologue HU from Bacillus stearothermophilus (HU Bst). Based on primary structure analysis, as well as on the results of mutational analysis of HU Bst ( T(m)=61.6 degrees C) and Bacillus subtilis (HU Bsu, T(m)=39.7 degrees C), we have designed and produced several single and combined mutations to study their effect on the thermostability of the recombinant HU Tmar. Among others, the triplet mutant HU Tmar-G15E/E34D/V42I ( T(m)=35.9 degrees C) has converted the extreme thermophilic protein HU Tmar to mesophilic, like HU Bsu. In an attempt to analyze the various mutants of HU Tmar, we crystallized the point mutation HU Tmar-E34D, in which Glu34 was replaced by Asp, similar to the mesophilic HU Bsu. The mutant has T(m)=72.9 degrees C, as measured by circular dichroism, 7.6 degrees C lower than the wild type. The crystal structure of HU Tmar-E34D was determined at 100 K and refined at 1.72 A resolution. A comparison with the wild-type structures clearly shows that two hydrogen bonds have been disrupted between Glu34 from one subunit and Thr13 from the other subunit, and vice versa. Our analysis points to this as the prime cause of the destabilization compared to the wild type. The three new structures were compared, together with the X-ray structure of a similar protein, HU Bst, with the aim of relating their structural properties and different thermal stability. The presented results show that the HU Tmar protein achieves its stability by employing a dual strategy. On the one hand, we observe local hydrophobic interactions, which stabilize the secondary structure elements, and on the other hand, electrostatic interactions between side chains. More... »

PAGES

111-122

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00792-002-0302-7

DOI

http://dx.doi.org/10.1007/s00792-002-0302-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1075259974

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12664263


Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
Incoming Citations Browse incoming citations for this publication using opencitations.net

JSON-LD is the canonical representation for SciGraph data.

TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

[
  {
    "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
    "about": [
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biochemistry and Cell Biology", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biological Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Amino Acid Sequence", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Bacillus subtilis", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Bacterial Proteins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Base Sequence", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Crystallography, X-Ray", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "DNA, Bacterial", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "DNA-Binding Proteins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Dimerization", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Drug Stability", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Geobacillus stearothermophilus", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Models, Molecular", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Molecular Sequence Data", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Mutagenesis, Site-Directed", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protein Folding", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protein Structure, Secondary", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protein Subunits", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Recombinant Proteins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Sequence Homology, Amino Acid", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Static Electricity", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Temperature", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Thermotoga maritima", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "National and Kapodistrian University of Athens", 
          "id": "https://www.grid.ac/institutes/grid.5216.0", 
          "name": [
            "National and Kapodistrian University of Athens, Faculty of Biology, Department of Biochemistry and Molecular Biology, Panepistimiopolis-Zographou, 157 84 Athens, Greece"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Christodoulou", 
        "givenName": "Evangelos", 
        "id": "sg:person.01010102466.94", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01010102466.94"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "University Medical Center Hamburg-Eppendorf", 
          "id": "https://www.grid.ac/institutes/grid.13648.38", 
          "name": [
            "Institute of Biochemistry and Molecular Biology, UKE, c/o DESY, Build.22a, Notkestrasse 85, 22603 Hamburg, Germany"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Rypniewski", 
        "givenName": "Wojciech R.", 
        "id": "sg:person.01022435553.16", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01022435553.16"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "National and Kapodistrian University of Athens", 
          "id": "https://www.grid.ac/institutes/grid.5216.0", 
          "name": [
            "National and Kapodistrian University of Athens, Faculty of Biology, Department of Biochemistry and Molecular Biology, Panepistimiopolis-Zographou, 157 84 Athens, Greece"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Vorgias", 
        "givenName": "Constantinos E.", 
        "id": "sg:person.012207207204.84", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.012207207204.84"
        ], 
        "type": "Person"
      }
    ], 
    "datePublished": "2003-04", 
    "datePublishedReg": "2003-04-01", 
    "description": "The histone-like DNA-binding proteins (HU) are a convenient model for studying factors affecting thermostability because of their relatively simple, easily comparable structures, their common function, and their presence in organisms of widely differing thermostability. We report the determination of the high-resolution structure (1.53 A) at 273 K and 100 K of the HU protein from the hyper-thermophilic eubacterium Thermotoga maritima(HU Tmar, T(m)=80.5 degrees C). The structural data presented clearly show that the HU Tmar has a fold similar to its thermophilic homologue HU from Bacillus stearothermophilus (HU Bst). Based on primary structure analysis, as well as on the results of mutational analysis of HU Bst ( T(m)=61.6 degrees C) and Bacillus subtilis (HU Bsu, T(m)=39.7 degrees C), we have designed and produced several single and combined mutations to study their effect on the thermostability of the recombinant HU Tmar. Among others, the triplet mutant HU Tmar-G15E/E34D/V42I ( T(m)=35.9 degrees C) has converted the extreme thermophilic protein HU Tmar to mesophilic, like HU Bsu. In an attempt to analyze the various mutants of HU Tmar, we crystallized the point mutation HU Tmar-E34D, in which Glu34 was replaced by Asp, similar to the mesophilic HU Bsu. The mutant has T(m)=72.9 degrees C, as measured by circular dichroism, 7.6 degrees C lower than the wild type. The crystal structure of HU Tmar-E34D was determined at 100 K and refined at 1.72 A resolution. A comparison with the wild-type structures clearly shows that two hydrogen bonds have been disrupted between Glu34 from one subunit and Thr13 from the other subunit, and vice versa. Our analysis points to this as the prime cause of the destabilization compared to the wild type. The three new structures were compared, together with the X-ray structure of a similar protein, HU Bst, with the aim of relating their structural properties and different thermal stability. The presented results show that the HU Tmar protein achieves its stability by employing a dual strategy. On the one hand, we observe local hydrophobic interactions, which stabilize the secondary structure elements, and on the other hand, electrostatic interactions between side chains.", 
    "genre": "research_article", 
    "id": "sg:pub.10.1007/s00792-002-0302-7", 
    "inLanguage": [
      "en"
    ], 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1116821", 
        "issn": [
          "1431-0651", 
          "1433-4909"
        ], 
        "name": "Extremophiles", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "2", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "7"
      }
    ], 
    "name": "High-resolution X-ray structure of the DNA-binding protein HU from the hyper-thermophilic Thermotoga maritima and the determinants of its thermostability", 
    "pagination": "111-122", 
    "productId": [
      {
        "name": "readcube_id", 
        "type": "PropertyValue", 
        "value": [
          "c969a8ead659d79741c700df1552a6f8f931621413d6758aa42cab7122662bf1"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "12664263"
        ]
      }, 
      {
        "name": "nlm_unique_id", 
        "type": "PropertyValue", 
        "value": [
          "9706854"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1007/s00792-002-0302-7"
        ]
      }, 
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1075259974"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1007/s00792-002-0302-7", 
      "https://app.dimensions.ai/details/publication/pub.1075259974"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2019-04-10T15:02", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000001_0000000264/records_8663_00000516.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "http://link.springer.com/10.1007%2Fs00792-002-0302-7"
  }
]
 

Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/s00792-002-0302-7'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/s00792-002-0302-7'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/s00792-002-0302-7'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/s00792-002-0302-7'


 

This table displays all metadata directly associated to this object as RDF triples.

170 TRIPLES      20 PREDICATES      50 URIs      42 LITERALS      30 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1007/s00792-002-0302-7 schema:about N0093d2183a9c4cd8babe2c5ed2d13831
2 N13c6399c5e0241d4914630a84a0ca588
3 N14507bb88b364acbb45457602052fa42
4 N3456f816947e4588bc5b8d2d4ee2e4d2
5 N3f7f06cde6414df0ab15424afed95089
6 N49db117f57a24c8584d723b3c17213e5
7 N55fbe0cb38464a4393c454a423e44fe4
8 N5e2b2918db8e4bbfb9afe45d38955de7
9 N5f87c9fa0d954aa7924e7ff70f3c4607
10 N692fb041fb2a450e89b964fc0f542f4b
11 N702fbb7c9d874ba0a772ef2d8da10719
12 N825748273f14467e92477fa810c75a3e
13 N88373acf026a4df79093fdd75584d679
14 N8b46f4053d274b0cb41ea94a57307b4b
15 Nd0369aa2e18f406a80c20ebaec30594d
16 Nd2405def64a44932875d2513f1f6a57d
17 Ne47f4873c6d9402fbe4946a4e5ea3210
18 Ne48e58222ca04fad85f25c1767fa3471
19 Ned99b71f0a354ce59be620abebff01f6
20 Nf04e2aaaef514bd9be67795809bf6e05
21 Nff81e353b019403b80bc15c60801e70f
22 anzsrc-for:06
23 anzsrc-for:0601
24 schema:author Ne8578d8e49614632a6d81bb52509a53b
25 schema:datePublished 2003-04
26 schema:datePublishedReg 2003-04-01
27 schema:description The histone-like DNA-binding proteins (HU) are a convenient model for studying factors affecting thermostability because of their relatively simple, easily comparable structures, their common function, and their presence in organisms of widely differing thermostability. We report the determination of the high-resolution structure (1.53 A) at 273 K and 100 K of the HU protein from the hyper-thermophilic eubacterium Thermotoga maritima(HU Tmar, T(m)=80.5 degrees C). The structural data presented clearly show that the HU Tmar has a fold similar to its thermophilic homologue HU from Bacillus stearothermophilus (HU Bst). Based on primary structure analysis, as well as on the results of mutational analysis of HU Bst ( T(m)=61.6 degrees C) and Bacillus subtilis (HU Bsu, T(m)=39.7 degrees C), we have designed and produced several single and combined mutations to study their effect on the thermostability of the recombinant HU Tmar. Among others, the triplet mutant HU Tmar-G15E/E34D/V42I ( T(m)=35.9 degrees C) has converted the extreme thermophilic protein HU Tmar to mesophilic, like HU Bsu. In an attempt to analyze the various mutants of HU Tmar, we crystallized the point mutation HU Tmar-E34D, in which Glu34 was replaced by Asp, similar to the mesophilic HU Bsu. The mutant has T(m)=72.9 degrees C, as measured by circular dichroism, 7.6 degrees C lower than the wild type. The crystal structure of HU Tmar-E34D was determined at 100 K and refined at 1.72 A resolution. A comparison with the wild-type structures clearly shows that two hydrogen bonds have been disrupted between Glu34 from one subunit and Thr13 from the other subunit, and vice versa. Our analysis points to this as the prime cause of the destabilization compared to the wild type. The three new structures were compared, together with the X-ray structure of a similar protein, HU Bst, with the aim of relating their structural properties and different thermal stability. The presented results show that the HU Tmar protein achieves its stability by employing a dual strategy. On the one hand, we observe local hydrophobic interactions, which stabilize the secondary structure elements, and on the other hand, electrostatic interactions between side chains.
28 schema:genre research_article
29 schema:inLanguage en
30 schema:isAccessibleForFree false
31 schema:isPartOf N0f5c2ba56ee644aaabc2e20a00325145
32 N11c386537bf0458cbe560e545757f2be
33 sg:journal.1116821
34 schema:name High-resolution X-ray structure of the DNA-binding protein HU from the hyper-thermophilic Thermotoga maritima and the determinants of its thermostability
35 schema:pagination 111-122
36 schema:productId N2fb66b48140b4cf3bbbeab492809e7da
37 N544b21246abe45deac7f3daeae52b08d
38 N93dbf26ca9ae4b6b99d1b6aff6cf6f77
39 Naa512788325f4593b0b8e0d01999d614
40 Nfd01fcd9708f456bb66b04a97f1031ba
41 schema:sameAs https://app.dimensions.ai/details/publication/pub.1075259974
42 https://doi.org/10.1007/s00792-002-0302-7
43 schema:sdDatePublished 2019-04-10T15:02
44 schema:sdLicense https://scigraph.springernature.com/explorer/license/
45 schema:sdPublisher Na7706c59f3264b09815b6482259d84b6
46 schema:url http://link.springer.com/10.1007%2Fs00792-002-0302-7
47 sgo:license sg:explorer/license/
48 sgo:sdDataset articles
49 rdf:type schema:ScholarlyArticle
50 N0093d2183a9c4cd8babe2c5ed2d13831 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
51 schema:name DNA-Binding Proteins
52 rdf:type schema:DefinedTerm
53 N0f5c2ba56ee644aaabc2e20a00325145 schema:issueNumber 2
54 rdf:type schema:PublicationIssue
55 N11c386537bf0458cbe560e545757f2be schema:volumeNumber 7
56 rdf:type schema:PublicationVolume
57 N13c6399c5e0241d4914630a84a0ca588 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
58 schema:name Bacillus subtilis
59 rdf:type schema:DefinedTerm
60 N14507bb88b364acbb45457602052fa42 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
61 schema:name Drug Stability
62 rdf:type schema:DefinedTerm
63 N2fb66b48140b4cf3bbbeab492809e7da schema:name nlm_unique_id
64 schema:value 9706854
65 rdf:type schema:PropertyValue
66 N3456f816947e4588bc5b8d2d4ee2e4d2 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
67 schema:name Geobacillus stearothermophilus
68 rdf:type schema:DefinedTerm
69 N3f7f06cde6414df0ab15424afed95089 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
70 schema:name Molecular Sequence Data
71 rdf:type schema:DefinedTerm
72 N49db117f57a24c8584d723b3c17213e5 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
73 schema:name Amino Acid Sequence
74 rdf:type schema:DefinedTerm
75 N544b21246abe45deac7f3daeae52b08d schema:name pubmed_id
76 schema:value 12664263
77 rdf:type schema:PropertyValue
78 N55fbe0cb38464a4393c454a423e44fe4 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
79 schema:name Base Sequence
80 rdf:type schema:DefinedTerm
81 N5e2b2918db8e4bbfb9afe45d38955de7 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
82 schema:name Mutagenesis, Site-Directed
83 rdf:type schema:DefinedTerm
84 N5f87c9fa0d954aa7924e7ff70f3c4607 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
85 schema:name Thermotoga maritima
86 rdf:type schema:DefinedTerm
87 N692fb041fb2a450e89b964fc0f542f4b schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
88 schema:name Protein Structure, Secondary
89 rdf:type schema:DefinedTerm
90 N702fbb7c9d874ba0a772ef2d8da10719 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
91 schema:name Sequence Homology, Amino Acid
92 rdf:type schema:DefinedTerm
93 N71b6a9cf68144821a7cae37887e9c765 rdf:first sg:person.012207207204.84
94 rdf:rest rdf:nil
95 N825748273f14467e92477fa810c75a3e schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
96 schema:name Protein Subunits
97 rdf:type schema:DefinedTerm
98 N88373acf026a4df79093fdd75584d679 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
99 schema:name Static Electricity
100 rdf:type schema:DefinedTerm
101 N88bb05fc16964c5eaed9f9afaea06263 rdf:first sg:person.01022435553.16
102 rdf:rest N71b6a9cf68144821a7cae37887e9c765
103 N8b46f4053d274b0cb41ea94a57307b4b schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
104 schema:name DNA, Bacterial
105 rdf:type schema:DefinedTerm
106 N93dbf26ca9ae4b6b99d1b6aff6cf6f77 schema:name dimensions_id
107 schema:value pub.1075259974
108 rdf:type schema:PropertyValue
109 Na7706c59f3264b09815b6482259d84b6 schema:name Springer Nature - SN SciGraph project
110 rdf:type schema:Organization
111 Naa512788325f4593b0b8e0d01999d614 schema:name doi
112 schema:value 10.1007/s00792-002-0302-7
113 rdf:type schema:PropertyValue
114 Nd0369aa2e18f406a80c20ebaec30594d schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
115 schema:name Protein Folding
116 rdf:type schema:DefinedTerm
117 Nd2405def64a44932875d2513f1f6a57d schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
118 schema:name Temperature
119 rdf:type schema:DefinedTerm
120 Ne47f4873c6d9402fbe4946a4e5ea3210 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
121 schema:name Bacterial Proteins
122 rdf:type schema:DefinedTerm
123 Ne48e58222ca04fad85f25c1767fa3471 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
124 schema:name Dimerization
125 rdf:type schema:DefinedTerm
126 Ne8578d8e49614632a6d81bb52509a53b rdf:first sg:person.01010102466.94
127 rdf:rest N88bb05fc16964c5eaed9f9afaea06263
128 Ned99b71f0a354ce59be620abebff01f6 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
129 schema:name Models, Molecular
130 rdf:type schema:DefinedTerm
131 Nf04e2aaaef514bd9be67795809bf6e05 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
132 schema:name Crystallography, X-Ray
133 rdf:type schema:DefinedTerm
134 Nfd01fcd9708f456bb66b04a97f1031ba schema:name readcube_id
135 schema:value c969a8ead659d79741c700df1552a6f8f931621413d6758aa42cab7122662bf1
136 rdf:type schema:PropertyValue
137 Nff81e353b019403b80bc15c60801e70f schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
138 schema:name Recombinant Proteins
139 rdf:type schema:DefinedTerm
140 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
141 schema:name Biological Sciences
142 rdf:type schema:DefinedTerm
143 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
144 schema:name Biochemistry and Cell Biology
145 rdf:type schema:DefinedTerm
146 sg:journal.1116821 schema:issn 1431-0651
147 1433-4909
148 schema:name Extremophiles
149 rdf:type schema:Periodical
150 sg:person.01010102466.94 schema:affiliation https://www.grid.ac/institutes/grid.5216.0
151 schema:familyName Christodoulou
152 schema:givenName Evangelos
153 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01010102466.94
154 rdf:type schema:Person
155 sg:person.01022435553.16 schema:affiliation https://www.grid.ac/institutes/grid.13648.38
156 schema:familyName Rypniewski
157 schema:givenName Wojciech R.
158 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01022435553.16
159 rdf:type schema:Person
160 sg:person.012207207204.84 schema:affiliation https://www.grid.ac/institutes/grid.5216.0
161 schema:familyName Vorgias
162 schema:givenName Constantinos E.
163 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.012207207204.84
164 rdf:type schema:Person
165 https://www.grid.ac/institutes/grid.13648.38 schema:alternateName University Medical Center Hamburg-Eppendorf
166 schema:name Institute of Biochemistry and Molecular Biology, UKE, c/o DESY, Build.22a, Notkestrasse 85, 22603 Hamburg, Germany
167 rdf:type schema:Organization
168 https://www.grid.ac/institutes/grid.5216.0 schema:alternateName National and Kapodistrian University of Athens
169 schema:name National and Kapodistrian University of Athens, Faculty of Biology, Department of Biochemistry and Molecular Biology, Panepistimiopolis-Zographou, 157 84 Athens, Greece
170 rdf:type schema:Organization
 




Preview window. Press ESC to close (or click here)


...