Glycerol-enhanced detection of a preferential structure latent in unstructured 1SS-variants of lysozyme

Four species of 1SS‐varinats of lysozyme were almost unstructured in water, judged from their near‐UV CD and 1H‐15N‐HSQC spectra. Some preferential structure might exist in such a disordered state, but the population of molecules in such a conformation must have been too small to be detected by spec...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biopolymers Jg. 97; H. 7; S. 539 - 549
Hauptverfasser:	Noda, Yasuo, Narama, Kuniaki, Kasai, Kenichi, Tachibana, Hideki, Segawa, Shin-ichi
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Hoboken Wiley Subscription Services, Inc., A Wiley Company 01.07.2012
Schlagworte:	1SS-variants of lysozyme chemical chaperones Circular Dichroism Glycerol - chemistry glycerol-enhanced detection Magnetic Resonance Spectroscopy Muramidase - chemistry NMR study of unstructured proteins Protein Conformation protein folding intermediates Spectrophotometry, Ultraviolet
ISSN:	0006-3525, 1097-0282
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Abstract	Four species of 1SS‐varinats of lysozyme were almost unstructured in water, judged from their near‐UV CD and 1H‐15N‐HSQC spectra. Some preferential structure might exist in such a disordered state, but the population of molecules in such a conformation must have been too small to be detected by spectroscopic methods. Indeed, our previous study showed that the addition of 30% glycerol induced the unstructured 2SS‐variant of lysozyme to form a native‐like structure. To extend this method to more disordered proteins, we attempted to detect some preferential structure latent in unstructured 1SS‐variants by the glycerol‐enhanced detection. Only in one molecular species of the four 1SS‐variants, 1SS[6‐127] containing a single disulfide bridge of Cys6‐Cys127, a preferential structure was found in the presence of 50% glycerol. It was detected by near‐UV CD measurements and the H/D exchange method combined with the NMR spectroscopy. The glycerol‐induced structure in 1SS[6‐127] was not localized only in the vicinity of Cys6‐Cys127, and largely protected regions distributed themselves among A‐, B‐, and C‐helices and Ile55 and Leu56. It was similar to the glycerol‐induced structure in 2SS[6‐127, 64‐80] containing two disulfide bridges of Cys6‐Cys127 and Cys64‐Cys80, although the former was less rigid than the latter. The role of A‐helix (residues 4–15) is proposed as an origin of excellent potential of Cys6‐Cys127 for inducing a tertiary structure in the α‐domain. © 2012 Wiley Periodicals, Inc. Biopolymers 97:539–549, 2012.
AbstractList	Four species of 1SS‐varinats of lysozyme were almost unstructured in water, judged from their near‐UV CD and 1H‐15N‐HSQC spectra. Some preferential structure might exist in such a disordered state, but the population of molecules in such a conformation must have been too small to be detected by spectroscopic methods. Indeed, our previous study showed that the addition of 30% glycerol induced the unstructured 2SS‐variant of lysozyme to form a native‐like structure. To extend this method to more disordered proteins, we attempted to detect some preferential structure latent in unstructured 1SS‐variants by the glycerol‐enhanced detection. Only in one molecular species of the four 1SS‐variants, 1SS[6‐127] containing a single disulfide bridge of Cys6‐Cys127, a preferential structure was found in the presence of 50% glycerol. It was detected by near‐UV CD measurements and the H/D exchange method combined with the NMR spectroscopy. The glycerol‐induced structure in 1SS[6‐127] was not localized only in the vicinity of Cys6‐Cys127, and largely protected regions distributed themselves among A‐, B‐, and C‐helices and Ile55 and Leu56. It was similar to the glycerol‐induced structure in 2SS[6‐127, 64‐80] containing two disulfide bridges of Cys6‐Cys127 and Cys64‐Cys80, although the former was less rigid than the latter. The role of A‐helix (residues 4–15) is proposed as an origin of excellent potential of Cys6‐Cys127 for inducing a tertiary structure in the α‐domain. © 2012 Wiley Periodicals, Inc. Biopolymers 97:539–549, 2012. Four species of 1SS‐varinats of lysozyme were almost unstructured in water, judged from their near‐UV CD and 1 H‐ 15 N‐HSQC spectra. Some preferential structure might exist in such a disordered state, but the population of molecules in such a conformation must have been too small to be detected by spectroscopic methods. Indeed, our previous study showed that the addition of 30% glycerol induced the unstructured 2SS‐variant of lysozyme to form a native‐like structure. To extend this method to more disordered proteins, we attempted to detect some preferential structure latent in unstructured 1SS‐variants by the glycerol‐enhanced detection. Only in one molecular species of the four 1SS‐variants, 1SS[6‐127] containing a single disulfide bridge of Cys6‐Cys127, a preferential structure was found in the presence of 50% glycerol. It was detected by near‐UV CD measurements and the H/D exchange method combined with the NMR spectroscopy. The glycerol‐induced structure in 1SS[6‐127] was not localized only in the vicinity of Cys6‐Cys127, and largely protected regions distributed themselves among A‐, B‐, and C‐helices and Ile55 and Leu56. It was similar to the glycerol‐induced structure in 2SS[6‐127, 64‐80] containing two disulfide bridges of Cys6‐Cys127 and Cys64‐Cys80, although the former was less rigid than the latter. The role of A‐helix (residues 4–15) is proposed as an origin of excellent potential of Cys6‐Cys127 for inducing a tertiary structure in the α‐domain. © 2012 Wiley Periodicals, Inc. Biopolymers 97:539–549, 2012. Four species of 1SS-varinats of lysozyme were almost unstructured in water, judged from their near-UV CD and (1) H-(15) N-HSQC spectra. Some preferential structure might exist in such a disordered state, but the population of molecules in such a conformation must have been too small to be detected by spectroscopic methods. Indeed, our previous study showed that the addition of 30% glycerol induced the unstructured 2SS-variant of lysozyme to form a native-like structure. To extend this method to more disordered proteins, we attempted to detect some preferential structure latent in unstructured 1SS-variants by the glycerol-enhanced detection. Only in one molecular species of the four 1SS-variants, 1SS[6-127] containing a single disulfide bridge of Cys6-Cys127, a preferential structure was found in the presence of 50% glycerol. It was detected by near-UV CD measurements and the H/D exchange method combined with the NMR spectroscopy. The glycerol-induced structure in 1SS[6-127] was not localized only in the vicinity of Cys6-Cys127, and largely protected regions distributed themselves among A-, B-, and C-helices and Ile55 and Leu56. It was similar to the glycerol-induced structure in 2SS[6-127, 64-80] containing two disulfide bridges of Cys6-Cys127 and Cys64-Cys80, although the former was less rigid than the latter. The role of A-helix (residues 4-15) is proposed as an origin of excellent potential of Cys6-Cys127 for inducing a tertiary structure in the α-domain. Four species of 1SS-varinats of lysozyme were almost unstructured in water, judged from their near-UV CD and (1) H-(15) N-HSQC spectra. Some preferential structure might exist in such a disordered state, but the population of molecules in such a conformation must have been too small to be detected by spectroscopic methods. Indeed, our previous study showed that the addition of 30% glycerol induced the unstructured 2SS-variant of lysozyme to form a native-like structure. To extend this method to more disordered proteins, we attempted to detect some preferential structure latent in unstructured 1SS-variants by the glycerol-enhanced detection. Only in one molecular species of the four 1SS-variants, 1SS[6-127] containing a single disulfide bridge of Cys6-Cys127, a preferential structure was found in the presence of 50% glycerol. It was detected by near-UV CD measurements and the H/D exchange method combined with the NMR spectroscopy. The glycerol-induced structure in 1SS[6-127] was not localized only in the vicinity of Cys6-Cys127, and largely protected regions distributed themselves among A-, B-, and C-helices and Ile55 and Leu56. It was similar to the glycerol-induced structure in 2SS[6-127, 64-80] containing two disulfide bridges of Cys6-Cys127 and Cys64-Cys80, although the former was less rigid than the latter. The role of A-helix (residues 4-15) is proposed as an origin of excellent potential of Cys6-Cys127 for inducing a tertiary structure in the α-domain.Four species of 1SS-varinats of lysozyme were almost unstructured in water, judged from their near-UV CD and (1) H-(15) N-HSQC spectra. Some preferential structure might exist in such a disordered state, but the population of molecules in such a conformation must have been too small to be detected by spectroscopic methods. Indeed, our previous study showed that the addition of 30% glycerol induced the unstructured 2SS-variant of lysozyme to form a native-like structure. To extend this method to more disordered proteins, we attempted to detect some preferential structure latent in unstructured 1SS-variants by the glycerol-enhanced detection. Only in one molecular species of the four 1SS-variants, 1SS[6-127] containing a single disulfide bridge of Cys6-Cys127, a preferential structure was found in the presence of 50% glycerol. It was detected by near-UV CD measurements and the H/D exchange method combined with the NMR spectroscopy. The glycerol-induced structure in 1SS[6-127] was not localized only in the vicinity of Cys6-Cys127, and largely protected regions distributed themselves among A-, B-, and C-helices and Ile55 and Leu56. It was similar to the glycerol-induced structure in 2SS[6-127, 64-80] containing two disulfide bridges of Cys6-Cys127 and Cys64-Cys80, although the former was less rigid than the latter. The role of A-helix (residues 4-15) is proposed as an origin of excellent potential of Cys6-Cys127 for inducing a tertiary structure in the α-domain.
Author	Narama, Kuniaki Tachibana, Hideki Segawa, Shin-ichi Noda, Yasuo Kasai, Kenichi
Author_xml	– sequence: 1 givenname: Yasuo surname: Noda fullname: Noda, Yasuo organization: Department of Physics, School of Science and Technology, Kwansei Gakuin University, Sanda 669-1337, Japan – sequence: 2 givenname: Kuniaki surname: Narama fullname: Narama, Kuniaki organization: Department of Physics, School of Science and Technology, Kwansei Gakuin University, Sanda 669-1337, Japan – sequence: 3 givenname: Kenichi surname: Kasai fullname: Kasai, Kenichi organization: Department of Physics, School of Science and Technology, Kwansei Gakuin University, Sanda 669-1337, Japan – sequence: 4 givenname: Hideki surname: Tachibana fullname: Tachibana, Hideki organization: Department of Biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, Kinokawa 649-6493, Japan – sequence: 5 givenname: Shin-ichi surname: Segawa fullname: Segawa, Shin-ichi email: shsegawa@kwansei.ac.jp organization: Department of Physics, School of Science and Technology, Kwansei Gakuin University, Sanda 669-1337, Japan
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/22344587$$D View this record in MEDLINE/PubMed
BookMark	eNp1kEtv1DAURi1URKctC_4A8g6xSOtXYnsJhU4rFagoj6XlcW7A4HGmtkOb_noyzEwXCFaWrs75ZJ0DtBf7CAg9o-SYEsJOFn51zBjh8hGaUaJlRZhie2hGCGkqXrN6Hx3k_IMQITglT9A-Y1yIWskZ-jYPo4PUhwridxsdtLiFAq74PuK-wxavEnSQIBZvA84lDa4MCXCwZbphH_EQH64tptfX1S-bvI0lr_0w5v5-XMIRetzZkOHp9j1En8_efjo9ry4_zC9OX11WTjAlK6slKCccwPTDhmktu1ZAC6Lruqa1pFbOOUYEo1rRTjrSKKYcByL5wtKG8UP0YrO7Sv3NALmYpc8OQrAR-iEbrbkmilI-kc-35LBYQmtWyS9tGs2uzQScbACX-pynCsb5YtdhSrI-GErMur6Z6ps_9Sfj5V_GbvRf7Hb91gcY_w-a1xdXO6PaGD4XuHswbPppGsllbb6-n5svzZuz-uNcm3f8N9EipAk
CitedBy_id	crossref_primary_10_3390_ijms140713194
Cites_doi	10.1063/1.2735620 10.1021/ja004206b 10.1021/bi00254a009 10.1021/bi00010a014 10.1021/bi00304a008 10.1021/bi992887l 10.1021/bi00447a051 10.1006/jmbi.1999.3442 10.1073/pnas.96.14.7899 10.1021/bi0113418 10.1038/nsb792 10.1093/emboj/18.17.4794 10.1021/ja00052a088 10.1002/(SICI)1521-3773(19980420)37:7<868::AID-ANIE868>3.0.CO;2-H 10.1016/0022-2364(90)90152-Y 10.1021/bi049967w 10.1002/prot.22103 10.1006/jmbi.1998.1825 10.1073/pnas.95.16.9268 10.1006/jmbi.1999.2915 10.1016/S0014-5793(00)01904-9 10.1002/bip.21198 10.1002/pro.5560040420 10.1002/cbic.200500196 10.1073/pnas.96.4.1262 10.1016/0014-5793(92)80466-T 10.1016/0263-7855(96)00018-5 10.1002/pro.5560070806 10.1002/prot.22430 10.1021/bi00519a023 10.1021/bi00120a019
ContentType	Journal Article
Copyright	Copyright © 2012 Wiley Periodicals, Inc.
Copyright_xml	– notice: Copyright © 2012 Wiley Periodicals, Inc.
DBID	BSCLL AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8
DOI	10.1002/bip.22037
DatabaseName	Istex CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic
DatabaseTitleList	CrossRef MEDLINE MEDLINE - Academic
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Chemistry
EISSN	1097-0282
EndPage	549
ExternalDocumentID	22344587 10_1002_bip_22037 BIP22037 ark_67375_WNG_V6DF5RG9_M
Genre	article Research Support, U.S. Gov't, Non-P.H.S Journal Article
GrantInformation_xml	– fundername: The “Open Research Project for Physical Science of Biomolecular Systems” and a matching subsidy “Academic Frontier Project for Private Universities” funderid: 21570173; 22570164
GroupedDBID	.GA .Y3 05W 10A 1OC 31~ 4.4 4ZD 51W 51X 52N 52O 52P 52T 52W 52X 7PT 930 A03 AANLZ AASGY AAXRX ACAHQ ACCZN ACXBN ADOZA AEUYR AFBPY AFZJQ ALMA_UNASSIGNED_HOLDINGS ALUQN AMYDB ATUGU BRXPI BSCLL BY8 DRFUL DRSTM G-S GNP GODZA HF~ HHZ LATKE LEEKS LITHE LOXES LP6 LP7 LUTES MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM P2W P4D QB0 UB1 WIH WIK WJL WQJ XG1 XV2 ZZTAW AAYXX CITATION O8X CGR CUY CVF ECM EIF NPM 7X8
ID	FETCH-LOGICAL-c4287-a97e8c4cee23462997fd4ede4fff6da058ccc20421981f7c06828c3e073ba1623
IEDL.DBID	DRFUL
ISICitedReferencesCount	2
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000302604300006&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	0006-3525
IngestDate	Fri Jul 11 11:12:32 EDT 2025 Thu Apr 03 07:05:19 EDT 2025 Sat Nov 29 05:39:30 EST 2025 Tue Nov 18 21:32:46 EST 2025 Wed Aug 20 07:27:06 EDT 2025 Tue Sep 09 05:32:11 EDT 2025
IsPeerReviewed	true
IsScholarly	true
Issue	7
Language	English
License	http://onlinelibrary.wiley.com/termsAndConditions#vor Copyright © 2012 Wiley Periodicals, Inc.
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c4287-a97e8c4cee23462997fd4ede4fff6da058ccc20421981f7c06828c3e073ba1623
Notes	ark:/67375/WNG-V6DF5RG9-M The "Open Research Project for Physical Science of Biomolecular Systems" and a matching subsidy "Academic Frontier Project for Private Universities" - No. 21570173; No. 22570164 istex:FA4924977EFBE8D85C43B6424702C15C770C7FFA ArticleID:BIP22037 This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
PMID	22344587
PQID	993908113
PQPubID	23479
PageCount	11
ParticipantIDs	proquest_miscellaneous_993908113 pubmed_primary_22344587 crossref_citationtrail_10_1002_bip_22037 crossref_primary_10_1002_bip_22037 wiley_primary_10_1002_bip_22037_BIP22037 istex_primary_ark_67375_WNG_V6DF5RG9_M
PublicationCentury	2000
PublicationDate	July 2012
PublicationDateYYYYMMDD	2012-07-01
PublicationDate_xml	– month: 07 year: 2012 text: July 2012
PublicationDecade	2010
PublicationPlace	Hoboken
PublicationPlace_xml	– name: Hoboken – name: United States
PublicationTitle	Biopolymers
PublicationTitleAlternate	Biopolymers
PublicationYear	2012
Publisher	Wiley Subscription Services, Inc., A Wiley Company
Publisher_xml	– name: Wiley Subscription Services, Inc., A Wiley Company
References	Hoshino, M.;Katou, H.;Hagihara, Y.;Hasegawa, K.;Naiki, H.;Goto, Y. Nat Struct Biol 2002, 9, 332-336. Humphrey, W.;Dalke, A.;Schulten, K. J Mol Graphics 1996, 14, 33-38. Knubovets, T.;Osterhout, J. J.;Connolly, P. J.;Klibanov, A. M. Proc Natl Acad Sci USA 1999, 96, 1262-1267. Zhang, Y.;Paterson, Y.;Roder, H. Protein Sci 1995, 4, 804-814. van den Berg, B.;Chung, E. W.;Robinson, C. V.;Mateo, P. L.;Dobson, C. M. EMBO J 1999, 18, 4794-4803. Sinibaldi, R.;Ortore, M. G.;Spinozzi, F.;Carsughi, F.;Frielinghaus, H.;Cinelli, S.;Onori, G.;Mariani, P. J Chem Phys 2007, 126, 235101-235109. Sawano, H.;Koumoto, Y.;Ohta, K.;Sasaki, Y.;Segawa, S.;Tachibana, H. FEBS Lett 1992, 303, 11-14. Wu, L. C.;Kim, P. S. J Mol Biol 1998, 280, 175-182. Tachibana, H.;Ohta, K.;Sawano, H.;Koumoto, Y.;Segawa, S. Biochemistry 1994, 33, 15008-15016. Creighton, T. E. Chapter 1 in Mechanisms of Protein Folding; Pain, R. H., Ed.; Oxford University Press, New York, 1994; pp 1-25. Dobson, C. M.;Sali, A.;Karplus, M. Angew Chem Int Ed 1998, 37, 868-893. Gekko, K.;Timasheff, S. N. Biochemistry 1981, 20, 4667-4676. Sakamoto, K.;Hirai, K.;Kitamura, Y.;Yamazaki, K.;Yusa, M.;Tokunaga, N.;Doi, G.;Noda, Y.;Tachibana, H.;Segawa, S. Biopolymers 2009, 91, 665-675. Chakshusmathi, G.;Ratnaparkhi, G. S.;Madhu, P. K.;Varadarajan, R. Proc Natl Acad Sci USA 1999, 96, 7899-7904. Noda, Y.;Yokota, A.;Horii, D.;Tominaga, T.;Tanisaka, Y.;Tachibana, H.;Segawa, S. Biochemistry 2002, 41, 2130-2139. Collins, E. S.;Wirmer, J.;Hirai, K.;Tachibana, H.;Segawa, S.;Dobson, C. M.;Schwalbe, H. ChemBioChem 2005, 6, 1619-1627. Zou, Q.;Bennion, B. J.;Daggett, V.;Murphy, K. P. J Am Chem Soc 2002, 124, 1192-1202. Lehmann, M. S.;Zaccai, G. Biochemistry 1984, 23, 1939- 1942. Frenkiel, T.;Bauer, C.;Carr, M. D.;Birdsall, B.;Feeney, J. J Magn Reson 1990, 90, 420-425. Yokota, A.;Takenaka, H.;Oh, T.;Noda, Y.;Segawa, S. Protein Sci 1998, 7, 1717-1727. Courtenay, E. S.;Capp, M. W.;Anderson, C. F.;Record, M. T.,Jr. Biochemistry 2000, 39, 4455-4471. Auton, M.;Bolen, D. W.;Rösgen, J. Proteins 2008, 73, 802-813. Tachibana, H. FEBS Lett 2000, 480, 175-178. Kay, L. E.;Keifer, P.;Saarinen, T. J Am Chem Soc 1992, 114, 10663-10665. Yokota, A.;Izutani, K.;Takai, M.;Kubo, Y.;Noda, Y.;Koumoto, Y.;Tachibana, H.;Segawa, S. J Mol Biol 2000, 295, 1275-1288. Matsuo, K.;Watanabe, H.;Tate, S.;Tachibana, H.;Gekko, K. Proteins 2009, 77, 191-201. Peng, Z.-y.;Wu, L. C.;Kim, P. S. Biochemistry 1995, 34, 3248-3252. van den Berg, B.;Chung, E. W.;Robinson C. V.;Dobson, C. M. J Mol Biol 1999, 290, 781-796. Qu, Y.;Bolen, C. L.;Bolen, D. W. Proc Natl Acad Sci USA 1998, 95, 9268-9273. Varadarajan, R.;Connelly, P. R.;Sturtevant, J. M.;Richards, F. M. Biochemistry, 1992, 31, 1421-1426. Manning, M. C.;Woody, R. W. Biochemistry 1989, 28, 8609-8613. Yokota, A.;Hirai, K.;Miyauchi, H.;Iimura, S.;Noda, Y.;Inoue, K.;Akasaka, K.;Tachibana, H.;Segawa, S. Biochemistry 2004, 43, 6663-6669. 2004; 43 2007; 126 1998; 280 2002; 9 1995; 34 1984; 23 1999; 290 1992; 303 2000; 295 1994 1996; 14 1992; 31 2008; 73 1995; 4 1981; 20 1989; 28 1998; 37 2009; 77 2000; 39 2002; 41 2009; 91 1999; 18 2002; 124 1992; 114 2000; 480 1994; 33 2005; 6 1999; 96 1998; 7 1998; 95 1990; 90 e_1_2_5_26_2 e_1_2_5_27_2 e_1_2_5_24_2 e_1_2_5_25_2 e_1_2_5_22_2 e_1_2_5_23_2 e_1_2_5_20_2 e_1_2_5_21_2 e_1_2_5_28_2 e_1_2_5_29_2 e_1_2_5_14_2 e_1_2_5_13_2 e_1_2_5_9_2 e_1_2_5_16_2 e_1_2_5_8_2 e_1_2_5_15_2 e_1_2_5_7_2 e_1_2_5_10_2 e_1_2_5_33_2 e_1_2_5_6_2 Creighton T. E. (e_1_2_5_2_2) 1994 e_1_2_5_5_2 e_1_2_5_12_2 e_1_2_5_31_2 e_1_2_5_4_2 e_1_2_5_11_2 e_1_2_5_32_2 e_1_2_5_3_2 e_1_2_5_18_2 e_1_2_5_17_2 e_1_2_5_19_2 e_1_2_5_30_2
References_xml	– reference: Peng, Z.-y.;Wu, L. C.;Kim, P. S. Biochemistry 1995, 34, 3248-3252. – reference: Lehmann, M. S.;Zaccai, G. Biochemistry 1984, 23, 1939- 1942. – reference: Wu, L. C.;Kim, P. S. J Mol Biol 1998, 280, 175-182. – reference: Courtenay, E. S.;Capp, M. W.;Anderson, C. F.;Record, M. T.,Jr. Biochemistry 2000, 39, 4455-4471. – reference: Zou, Q.;Bennion, B. J.;Daggett, V.;Murphy, K. P. J Am Chem Soc 2002, 124, 1192-1202. – reference: Tachibana, H.;Ohta, K.;Sawano, H.;Koumoto, Y.;Segawa, S. Biochemistry 1994, 33, 15008-15016. – reference: Dobson, C. M.;Sali, A.;Karplus, M. Angew Chem Int Ed 1998, 37, 868-893. – reference: Gekko, K.;Timasheff, S. N. Biochemistry 1981, 20, 4667-4676. – reference: van den Berg, B.;Chung, E. W.;Robinson C. V.;Dobson, C. M. J Mol Biol 1999, 290, 781-796. – reference: Yokota, A.;Takenaka, H.;Oh, T.;Noda, Y.;Segawa, S. Protein Sci 1998, 7, 1717-1727. – reference: Hoshino, M.;Katou, H.;Hagihara, Y.;Hasegawa, K.;Naiki, H.;Goto, Y. Nat Struct Biol 2002, 9, 332-336. – reference: Manning, M. C.;Woody, R. W. Biochemistry 1989, 28, 8609-8613. – reference: Frenkiel, T.;Bauer, C.;Carr, M. D.;Birdsall, B.;Feeney, J. J Magn Reson 1990, 90, 420-425. – reference: Sinibaldi, R.;Ortore, M. G.;Spinozzi, F.;Carsughi, F.;Frielinghaus, H.;Cinelli, S.;Onori, G.;Mariani, P. J Chem Phys 2007, 126, 235101-235109. – reference: Humphrey, W.;Dalke, A.;Schulten, K. J Mol Graphics 1996, 14, 33-38. – reference: Yokota, A.;Hirai, K.;Miyauchi, H.;Iimura, S.;Noda, Y.;Inoue, K.;Akasaka, K.;Tachibana, H.;Segawa, S. Biochemistry 2004, 43, 6663-6669. – reference: Matsuo, K.;Watanabe, H.;Tate, S.;Tachibana, H.;Gekko, K. Proteins 2009, 77, 191-201. – reference: Qu, Y.;Bolen, C. L.;Bolen, D. W. Proc Natl Acad Sci USA 1998, 95, 9268-9273. – reference: Noda, Y.;Yokota, A.;Horii, D.;Tominaga, T.;Tanisaka, Y.;Tachibana, H.;Segawa, S. Biochemistry 2002, 41, 2130-2139. – reference: van den Berg, B.;Chung, E. W.;Robinson, C. V.;Mateo, P. L.;Dobson, C. M. EMBO J 1999, 18, 4794-4803. – reference: Collins, E. S.;Wirmer, J.;Hirai, K.;Tachibana, H.;Segawa, S.;Dobson, C. M.;Schwalbe, H. ChemBioChem 2005, 6, 1619-1627. – reference: Kay, L. E.;Keifer, P.;Saarinen, T. J Am Chem Soc 1992, 114, 10663-10665. – reference: Auton, M.;Bolen, D. W.;Rösgen, J. Proteins 2008, 73, 802-813. – reference: Creighton, T. E. Chapter 1 in Mechanisms of Protein Folding; Pain, R. H., Ed.; Oxford University Press, New York, 1994; pp 1-25. – reference: Yokota, A.;Izutani, K.;Takai, M.;Kubo, Y.;Noda, Y.;Koumoto, Y.;Tachibana, H.;Segawa, S. J Mol Biol 2000, 295, 1275-1288. – reference: Knubovets, T.;Osterhout, J. J.;Connolly, P. J.;Klibanov, A. M. Proc Natl Acad Sci USA 1999, 96, 1262-1267. – reference: Tachibana, H. FEBS Lett 2000, 480, 175-178. – reference: Sakamoto, K.;Hirai, K.;Kitamura, Y.;Yamazaki, K.;Yusa, M.;Tokunaga, N.;Doi, G.;Noda, Y.;Tachibana, H.;Segawa, S. Biopolymers 2009, 91, 665-675. – reference: Zhang, Y.;Paterson, Y.;Roder, H. Protein Sci 1995, 4, 804-814. – reference: Sawano, H.;Koumoto, Y.;Ohta, K.;Sasaki, Y.;Segawa, S.;Tachibana, H. FEBS Lett 1992, 303, 11-14. – reference: Chakshusmathi, G.;Ratnaparkhi, G. S.;Madhu, P. K.;Varadarajan, R. Proc Natl Acad Sci USA 1999, 96, 7899-7904. – reference: Varadarajan, R.;Connelly, P. R.;Sturtevant, J. M.;Richards, F. M. Biochemistry, 1992, 31, 1421-1426. – volume: 20 start-page: 4667 year: 1981 end-page: 4676 publication-title: Biochemistry – volume: 96 start-page: 7899 year: 1999 end-page: 7904 publication-title: Proc Natl Acad Sci USA – volume: 14 start-page: 33 year: 1996 end-page: 38 publication-title: J Mol Graphics – volume: 295 start-page: 1275 year: 2000 end-page: 1288 publication-title: J Mol Biol – volume: 7 start-page: 1717 year: 1998 end-page: 1727 publication-title: Protein Sci – volume: 77 start-page: 191 year: 2009 end-page: 201 publication-title: Proteins – volume: 33 start-page: 15008 year: 1994 end-page: 15016 publication-title: Biochemistry – volume: 280 start-page: 175 year: 1998 end-page: 182 publication-title: J Mol Biol – volume: 124 start-page: 1192 year: 2002 end-page: 1202 publication-title: J Am Chem Soc – volume: 114 start-page: 10663 year: 1992 end-page: 10665 publication-title: J Am Chem Soc – volume: 34 start-page: 3248 year: 1995 end-page: 3252 publication-title: Biochemistry – volume: 290 start-page: 781 year: 1999 end-page: 796 publication-title: J Mol Biol – volume: 23 start-page: 1939 year: 1984 end-page: 1942 publication-title: Biochemistry – volume: 28 start-page: 8609 year: 1989 end-page: 8613 publication-title: Biochemistry – volume: 126 start-page: 235101 year: 2007 end-page: 235109 publication-title: J Chem Phys – volume: 6 start-page: 1619 year: 2005 end-page: 1627 publication-title: ChemBioChem – volume: 480 start-page: 175 year: 2000 end-page: 178 publication-title: FEBS Lett – volume: 4 start-page: 804 year: 1995 end-page: 814 publication-title: Protein Sci – volume: 39 start-page: 4455 year: 2000 end-page: 4471 publication-title: Biochemistry – volume: 9 start-page: 332 year: 2002 end-page: 336 publication-title: Nat Struct Biol – start-page: 1 year: 1994 end-page: 25 – volume: 37 start-page: 868 year: 1998 end-page: 893 publication-title: Angew Chem Int Ed – volume: 96 start-page: 1262 year: 1999 end-page: 1267 publication-title: Proc Natl Acad Sci USA – volume: 41 start-page: 2130 year: 2002 end-page: 2139 publication-title: Biochemistry – volume: 91 start-page: 665 year: 2009 end-page: 675 publication-title: Biopolymers – volume: 95 start-page: 9268 year: 1998 end-page: 9273 publication-title: Proc Natl Acad Sci USA – volume: 43 start-page: 6663 year: 2004 end-page: 6669 publication-title: Biochemistry – volume: 18 start-page: 4794 year: 1999 end-page: 4803 publication-title: EMBO J – volume: 303 start-page: 11 year: 1992 end-page: 14 publication-title: FEBS Lett – volume: 31 start-page: 1421 year: 1992 end-page: 1426 publication-title: Biochemistry – volume: 73 start-page: 802 year: 2008 end-page: 813 publication-title: Proteins – volume: 90 start-page: 420 year: 1990 end-page: 425 publication-title: J Magn Reson – ident: e_1_2_5_13_2 doi: 10.1063/1.2735620 – ident: e_1_2_5_18_2 doi: 10.1021/ja004206b – ident: e_1_2_5_23_2 doi: 10.1021/bi00254a009 – ident: e_1_2_5_27_2 doi: 10.1021/bi00010a014 – ident: e_1_2_5_11_2 doi: 10.1021/bi00304a008 – ident: e_1_2_5_17_2 doi: 10.1021/bi992887l – ident: e_1_2_5_26_2 doi: 10.1021/bi00447a051 – ident: e_1_2_5_4_2 doi: 10.1006/jmbi.1999.3442 – ident: e_1_2_5_14_2 doi: 10.1073/pnas.96.14.7899 – ident: e_1_2_5_5_2 doi: 10.1021/bi0113418 – ident: e_1_2_5_22_2 doi: 10.1038/nsb792 – ident: e_1_2_5_33_2 doi: 10.1093/emboj/18.17.4794 – ident: e_1_2_5_24_2 doi: 10.1021/ja00052a088 – ident: e_1_2_5_3_2 doi: 10.1002/(SICI)1521-3773(19980420)37:7<868::AID-ANIE868>3.0.CO;2-H – ident: e_1_2_5_25_2 doi: 10.1016/0022-2364(90)90152-Y – ident: e_1_2_5_6_2 doi: 10.1021/bi049967w – ident: e_1_2_5_16_2 doi: 10.1002/prot.22103 – ident: e_1_2_5_28_2 doi: 10.1006/jmbi.1998.1825 – start-page: 1 volume-title: Mechanisms of Protein Folding year: 1994 ident: e_1_2_5_2_2 – ident: e_1_2_5_15_2 doi: 10.1073/pnas.95.16.9268 – ident: e_1_2_5_32_2 doi: 10.1006/jmbi.1999.2915 – ident: e_1_2_5_20_2 doi: 10.1016/S0014-5793(00)01904-9 – ident: e_1_2_5_7_2 doi: 10.1002/bip.21198 – ident: e_1_2_5_21_2 doi: 10.1002/pro.5560040420 – ident: e_1_2_5_8_2 doi: 10.1002/cbic.200500196 – ident: e_1_2_5_12_2 doi: 10.1073/pnas.96.4.1262 – ident: e_1_2_5_19_2 doi: 10.1016/0014-5793(92)80466-T – ident: e_1_2_5_29_2 doi: 10.1016/0263-7855(96)00018-5 – ident: e_1_2_5_31_2 doi: 10.1002/pro.5560070806 – ident: e_1_2_5_9_2 doi: 10.1002/prot.22430 – ident: e_1_2_5_10_2 doi: 10.1021/bi00519a023 – ident: e_1_2_5_30_2 doi: 10.1021/bi00120a019
SSID	ssj0044310 ssj0011473
Score	2.0101504
Snippet	Four species of 1SS‐varinats of lysozyme were almost unstructured in water, judged from their near‐UV CD and 1H‐15N‐HSQC spectra. Some preferential structure... Four species of 1SS‐varinats of lysozyme were almost unstructured in water, judged from their near‐UV CD and 1 H‐ 15 N‐HSQC spectra. Some preferential... Four species of 1SS-varinats of lysozyme were almost unstructured in water, judged from their near-UV CD and (1) H-(15) N-HSQC spectra. Some preferential...
SourceID	proquest pubmed crossref wiley istex
SourceType	Aggregation Database Index Database Enrichment Source Publisher
StartPage	539
SubjectTerms	1SS-variants of lysozyme chemical chaperones Circular Dichroism Glycerol - chemistry glycerol-enhanced detection Magnetic Resonance Spectroscopy Muramidase - chemistry NMR study of unstructured proteins Protein Conformation protein folding intermediates Spectrophotometry, Ultraviolet
Title	Glycerol-enhanced detection of a preferential structure latent in unstructured 1SS-variants of lysozyme
URI	https://api.istex.fr/ark:/67375/WNG-V6DF5RG9-M/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fbip.22037 https://www.ncbi.nlm.nih.gov/pubmed/22344587 https://www.proquest.com/docview/993908113
Volume	97
WOSCitedRecordID	wos000302604300006&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVWIB databaseName: Wiley Online Library Full Collection 2020 customDbUrl: eissn: 1097-0282 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0044310 issn: 0006-3525 databaseCode: DRFUL dateStart: 19960101 isFulltext: true titleUrlDefault: https://onlinelibrary.wiley.com providerName: Wiley-Blackwell – providerCode: PRVWIB databaseName: Wiley Online Library Full Collection 2020 customDbUrl: eissn: 1097-0282 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0011473 issn: 0006-3525 databaseCode: DRFUL dateStart: 19960101 isFulltext: true titleUrlDefault: https://onlinelibrary.wiley.com providerName: Wiley-Blackwell
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9QwEB61u0hw4f1YHpWFEOpl6cbrxI44QcsuSGVVtbTszXJsR6wanNU-KpYTP4HfyC9h7DxQpSIhcYui0SSZGc98E49nAF4YnRqmaYRpicj7zHBcc4MEFSJyNCjNMh4aaZ8d8slETKfp0Ra8bs7CVP0h2h9ufmUEf-0XuMqWe3-ahmaz-StKB0O-DV2Kdss60D04Hp0etpsIEeOtV2YYKKvjKL7WK6Zx02VoQPdaTpdiU9eL-dtVwPMyjg2BaHTrvz7hNtys8Sd5UxnMHdiy7i5c32_Gvt2D83Gx0XZRFr9-_LTuSygQIMauQsmWI2VOFJnXw0nQOxSk6kC7XlhSIG51KzJzZO3au4ZEJyfI6wKTcl9z4zkUm2X5ffPV3ofT0btP--_79USGvvapVV-l3ArNMLDSIUswkvHcMGssy_M8MWoQC601RT8QpSLKuUatU6GHFtWeqQiR1gPouNLZR0A05TpGtMNsJpjIrGIcc2KKoSNRJmFpD3YbXUhdtyv3UzMKWTVaphKlJ4P0evC8JZ1XPTquInoZFNpSqMW5L2rjsfw8Gcuz5GAUH49T-bEHpNG4RNH7_RPlbLleSoRyKSKoaNiDh5UltMwQZDEWC3zKblD4399Dvv1wFC4e_zvpE7iBOK2uEn4KHdSgfQbX9MVqtlzswDafip3a-H8DdFsGeg
linkProvider	Wiley-Blackwell
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Zb9QwEB6VXaTywg1dTgsh1JelG68TOxIv0LLbiu2q6v1mJbajrhqc1R4VyxM_gd_IL2HsHKhSkZB4iyJrksz5jT2ZAXirVayZogGmJSLrMs3R5noRCkRkqFCKpdw30j4d8fFYnJ_HB2vwof4XpuwP0Wy4Ocvw_toZuNuQ3vrTNTSdTN9T2uvzW9BmqEZhC9o7h4OTUXOKEDDeuGWGkbL8H8UVe4U0rNsM9ehWQ-lacGo7Pn-7CXleB7I-Eg3u_d833Ie7FQIlH0uVeQBrxj6E9e168NsjuBzmK2VmRf7rx09jL3yJANFm4Yu2LCkykpBpNZ4E_UNOyh60y5khOSJXuyATS5a2uatJcHSEtK4wLXdVN45CvpoX31dfzWM4GXw-3t7tVjMZusolV90k5kYohqGV9lmEsYxnmhltWJZlkU56oVBKUfQEQSyCjCuUOxWqb1DwaRIg1noCLVtYswFEUa5CxDvMpIKJ1CSMY1ZMMXhEiY5Y3IHNWhhSVQ3L3dyMXJatlqlE7knPvQ68aZZOyy4dNy165yXarEhml66sjYfybDyUp9HOIDwcxnK_A6QWuUTWuxOUxJpiOZcI5mLEUEG_A09LVWiIIcxiLBT4lE0v8b-_h_y0d-Avnv370tewvnu8P5KjvfGX53AHUVtVM_wCWihN8xJuq6vFZD57VdnAb-_3CYI
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Zb9NAEB6VBgEv3Ec4VwihvoTGm7V3LfECDQ4VIYpaWvq2svcQUc06ylERnvgJ_EZ-CbO-UKUiIfFmWaOxPbMz8413dgbghVaxZooGmJYI22Oao831I1SIsLigFMt42Uj7eMwnE3FyEk-34HVzFqbqD9H-cPOWUfprb-Bmru3un66h2Wz-itL-gF-CDgvjCM2yMzxIjsbtLkLAeOuWGUbK6jyKL_YKadi0GerT3ZbTueDU8XL-dhHyPA9ky0iU3Pi_b7gJ12sESt5US-YWbBl3G67uNYPf7sDpKN8osyjyXz9-GvelLBEg2qzKoi1HCktSMq_Hk6B_yEnVg3a9MCRH5OpWZObI2rV3NQkOD5HXGablvurGc8g3y-L75qu5C0fJu09773v1TIae8slVL425EYphaKUDFmEs41Yzow2z1kY67YdCKUXREwSxCCxXqHcq1MCg4rM0QKx1D7Zd4cwDIIpyFSLeYSYTTGQmZRyzYorBI0p1xOIu7DTKkKpuWO7nZuSyarVMJUpPltLrwvOWdF516biI6GWp0ZYiXZz6sjYeys-TkTyOhkl4MIrlxy6QRuUSRe93UFJnivVSIpiLEUMFgy7cr5ZCywxhFmOhwKfslBr_-3vIt_vT8uLhv5M-gyvTYSLH-5MPj-Aagra6ZPgxbKMyzRO4rM5Ws-XiaW0CvwFvAgj9
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Glycerol-enhanced+detection+of+a+preferential+structure+latent+in+unstructured+1SS-variants+of+lysozyme&rft.jtitle=Biopolymers&rft.au=Noda%2C+Yasuo&rft.au=Narama%2C+Kuniaki&rft.au=Kasai%2C+Kenichi&rft.au=Tachibana%2C+Hideki&rft.date=2012-07-01&rft.issn=0006-3525&rft.volume=97&rft.issue=7&rft.spage=539&rft_id=info:doi/10.1002%2Fbip.22037&rft_id=info%3Apmid%2F22344587&rft.externalDocID=22344587
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-3525&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-3525&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-3525&client=summon