Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy (2017)
- Authors:
- USP affiliated authors: ARAUJO, ANA PAULA ULIAN DE - IFSC ; LOPES, JOSÉ LUIZ DE SOUZA - IF
- USP Schools: IFSC; IF
- DOI: 10.1007/s12551-017-0314-2
- Subjects: ESPECTROSCOPIA; PROTEÍNAS
- Keywords: Circular dichroism spectroscopy; Conformational changes; Protein conformation; Protein secondary structure; Synchrotron radiation circular dichroism spectroscopy
- Language: Inglês
- Imprenta:
- Publisher: Springer
- Publisher place: Heidelberg
- Date published: 2017
- Source:
- Título do periódico: Biophysical Reviews
- ISSN: 1867-2450
- Volume/Número/Paginação/Ano: v. 9, n. 5, p. 517-527, Oct. 2017
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: green
- Melhor URL em Acesso Aberto:
- Página do artigo
- Link para o PDF
- Evidência: oa repository (via OAI-PMH title and first author match)
- Licença:
- Versão: publishedVersion
- Tipo de hospedagem: repository
- Outras alternativas de URLs em Acesso Aberto:
- Página do artigo
- Link para o PDF
- Evidência: oa repository (via OAI-PMH title and first author match)
- Licença:
- Versão: publishedVersion
- Tipo de hospedagem: repository
-
Título: Biophysical Reviews
ISSN: 1867-2450
Citescore - 2017: 2.19
SJR - 2017: 0.822
SNIP - 2017: 0.557
-
ABNT
KUMAGAI, Patricia S.; ARAÚJO, Ana Paula Ulian de; LOPES, José Luiz de Souza. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy. Biophysical Reviews, Heidelberg, Springer, v. 9, n. 5, p. 517-527, 2017. Disponível em: < http://dx.doi.org/10.1007/s12551-017-0314-2 > DOI: 10.1007/s12551-017-0314-2. -
APA
Kumagai, P. S., Araújo, A. P. U. de, & Lopes, J. L. de S. (2017). Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy. Biophysical Reviews, 9( 5), 517-527. doi:10.1007/s12551-017-0314-2 -
NLM
Kumagai PS, Araújo APU de, Lopes JL de S. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy [Internet]. Biophysical Reviews. 2017 ; 9( 5): 517-527.Available from: http://dx.doi.org/10.1007/s12551-017-0314-2 -
Vancouver
Kumagai PS, Araújo APU de, Lopes JL de S. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy [Internet]. Biophysical Reviews. 2017 ; 9( 5): 517-527.Available from: http://dx.doi.org/10.1007/s12551-017-0314-2 - Anaerobaculum hydrogeniformans esterase (ahest): a new thermostable esterase for biotechnological applications
- Challenges in studying intrinsically disordered proteins
- Synchrotron radiation circular dichroism spectroscopy: advantages over conventional method
- Plantaricina 149 e análogos: atividade antimicrobiana, estudos estruturais e mecanismos de ação
- Purificação e investigação das propriedades físico-químicas de inibidores de proteases extraídos de sementes de Acacia plumosa Lowe
- Environmental factors modulating the stability and enzymatic activity of the Petrotoga mobilis Esterase (PmEst)
- Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response
- Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins
- A trypsin inhibitor purified from Cassia leiandra seeds has insecticidal activity against Aedes aegypti
- Frog foam nest protein diversity and synthesis
Informações sobre o DOI: 10.1007/s12551-017-0314-2 (Fonte: oaDOI API)
Versões disponíveis em Acesso Aberto do: 10.1007/s12551-017-0314-2 (Fonte: Unpaywall API)
Título do periódico: Biophysical Reviews
ISSN: 1867-2450,1867-2469
Informações sobre o Citescore
Biblioteca | Cód. de barras | Núm. de chamada |
---|---|---|
IFSC | 89026871 | PROD026871 |
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
Referências citadas na obra
Bremer A, Wolff M, Thalhammer A, Hincha DK (2017) Folding of intrinsically disordered plant LEA proteins is driven by glycerol-induced crowding and the presence of membranes. FEBS J 284(6):919–936. doi: 10.1111/febs.14023 |
---|
Bürck J, Wadhwani P, Fanghänel S, Ulrich AS (2016) Oriented circular dichroism: A method to characterize membrane-active peptides in oriented lipid bilayers. Acc Chem Res 49(2):184–192. doi: 10.1021/acs.accounts.5b00346 |
Cowieson NP, Miles AJ, Robin G, Forwood JK, Kobe B, Martin JL, Wallace BA (2008) Evaluating protein:protein complex formation using synchrotron radiation circular dichroism spectroscopy. Proteins 70(4):1142–1146 |
Drechsler A, Miles AJ, Norton RS, Wallace BA, Separovic F (2009) Effect of lipid on the conformation of the N-terminal region of equinatoxin II: A synchrotron radiation circular dichroism spectroscopic study. Eur Biophys J 39(1):121–127. doi: 10.1007/s00249-009-0445-x |
Feng Y, Yu W, Li X, Zhou Y, Hu J, Liu X (2013) Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins. J Biol Chem 288(39):28418–28427. doi: 10.1074/jbc.M113.478024 |
Garcia AF, Garcia W, Nonato MC, Araújo AP (2008) Structural stability and reversible unfolding of recombinant porcine S100A12. Biophys Chem 134(3):246–253. doi: 10.1016/j.bpc.2008.02.013 |
Garcia AF, Lopes JLS, Costa-Filho AJ, Wallace BA, Araujo APU (2013) Membrane interactions of S100A12 (Calgranulin C). PLoS One 8(12):e82555. doi: 10.1371/journal.pone.0082555 |
Greenfield NJ (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1(6):2876–2890. doi: 10.1038/nprot.2006.202 |
Hussain R, Jávorfi T, Rudd TR, Siligardi G (2016) High-throughput SRCD using multi-well plates and its applications. Sci Rep 6:38028. doi: 10.1038/srep38028 |
Jasanoff A, Fersht AR (1997) Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemist 36:8413. doi: 10.1021/bi9707133 |
Kelly SM, Jess TJ, Price NC (2005) How to study proteins by circular dichroism. Biochim Biophys Acta 1751(2):119–139 |
Kinseth MA, Anjard C, Fuller D, Guizzunti G, Loomis WF, Malhotra V (2007) The Golgi-associated protein GRASP is required for unconventional protein secretion during development. Cell 130:524–534. doi: 10.1016/j.cell.2007.06.029 |
Kumagai PS, DeMarco R, Lopes JLS (2017) Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. Eur Biophys J. doi 10.1007/s00249-017-1202-1 |
Lees JG, Miles AJ, Wien F, Wallace BA (2006) A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22(16):1955–1962 |
Lima MA, Hughes AJ, Veraldi N, Rudd TR, Hussain R, Brio AS, Chavante SF, Tersariol II, Siligardi G, Nader HB, Yates EA (2013) Antithrombin stabilisation by sulfated carbohydrates correlates with anticoagulant activity. Med Chem Commun 4:870–873. doi: 10.1039/C3MD00048F |
Lopes JLS, Miles AJ, Whitmore L, Wallace BA (2014a) Distinct circular dichroism spectroscopic signatures of polyproline II and unordered secondary structures: Applications in secondary structure analyses. Protein Sci 23(12):1765–1772. doi: 10.1002/pro.2558 |
Lopes JLS, Nobre TM, Cilli EM, Beltramini LM, Araujo APU, Wallace BA (2014b) Deconstructing the DGAT1 enzyme: Binding sites and substrate interactions. Biochim Biophys Acta 1838(12):3145–3152. doi: 10.1016/j.bbamem.2014.08.017 |
Lopes JLS, Orcia D, Araujo APU, DeMarco R, Wallace BA (2013) Folding factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14). Biophys J 104(11):2512–2520. doi: 10.1016/j.bpj.2013.03.063 |
Lopes JLS, Yoneda JS, Martins JM, DeMarco R, Jameson DM, Castro AM, Bossolan NR, Wallace BA, Araujo APU (2016) Environmental factors modulating the stability and enzymatic activity of the Petrotoga mobilis esterase (PmEst). PLoS One 11(6):e0158146. doi: 10.1371/journal.pone.0158146 |
Matsuo K, Gekko K (2013) Circular-dichroism and synchrotron-radiation circular-dichroism spectroscopy as tools to monitor protein structure in a lipid environment. Methods Mol Biol 974:151–176. doi: 10.1007/978-1-62703-275-9_8 |
Mendes LFS, Garcia AF, Kumagai PS, Morais FR, Melo FA, Kmetzsch L, Vainstein MH, Rodrigues ML, Costa-Filho AJ (2016) New structural insights into Golgi reassembly and stacking protein (GRASP) in solution. Sci Rep 6:29976. doi: 10.1038/srep29976 |
Micsonai A, Wien F, Kernya L, Lee YH, Goto Y, Réfrégiers M, Kardos J (2015) Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy. Proc Natl Acad Sci USA 112(24):E3095–E3103. doi: 10.1073/pnas.1500851112 |
Miles AJ, Drechsler A, Kristan K, Anderluh G, Norton RS, Wallace BA, Separovic F (2008) The effects of lipids on the structure of the eukaryotic cytolysin equinatoxin II: A synchrotron radiation circular dichroism spectroscopic study. Biochim Biophys Acta 1778(10):2091–2096. doi: 10.1016/j.bbamem.2008.04.001 |
Miles AJ, Wallace BA (2016) Circular dichroism spectroscopy of membrane proteins. Chem Soc Rev 45(18):4859–4872. doi: 10.1039/c5cs00084j |
Miller WC, Miles AJ, Wallace BA (2016) Structure of the C-terminal domain of the prokaryotic sodium channel orthologue NsvBa. Eur Biophys J 45(8):807–814 |
Orcia D, Zeraik AE, Lopes JLS, Macedo JNA, Santos CR, Oliveira KC, Anderson L, Wallace BA, Verjovski-Almeida S, Araujo APU, DeMarco R (2017) Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. Biochim Biophys Acta 1861(1 Pt A):3490–3497. doi: 10.1016/j.bbagen.2016.09.015 |
Orengo CA, Michie AD, Jones S, Jones DT, Swindells MB, Thornton JM (1997) CATH-a hierarchic classification of protein domain structures. Structure 5(8):1093–1108 |
Poklar Ulrih N (2017) Analytical techniques for the study of polyphenol-protein interactions. Crit Rev Food Sci Nutr 57(10):2144–2161. doi: 10.1080/10408398.2015.1052040 |
Powl AP, O’Reilly AO, Miles AJ, Wallace BA (2010) Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly. Proc Natl Acad Sci USA 107(32):14064–14069. doi: 10.1073/pnas.1001793107 |
Ranjbar B, Gill P (2009) Circular dichroism techniques: Biomolecular and nanostructural analyses- a review. Chem Biol Drug Des 74(2):101–120. doi: 10.1111/j.1747-0285.2009.00847.x |
Recveur-Brechot V, Bourhis JM, Uversky VN, Canard B, Longhi S (2006) Assessing protein disorder and induced folding. Proteins 62:24–45 |
Ruskamo S, Chukhlieb M, Vahokoski J, Bhargav SP, Liang F, Kursula I, Kursula P (2012) Juxtanodin is an intrinsically disordered F-actin-binding protein. Sci Rep 2:899. doi: 10.1038/srep00899 |
Sreerama N, Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287(2):252–260 |
Sutherland JC, Emrick A, France LL, Monteleone DC, Trunk J (1992) Circular dichroism user facility at the National Synchrotron Light Source: Estimation of protein secondary structure. BioTechniques 13(4):588–590 |
Truschel ST, Sengupta D, Foote A, Heroux A, Macbeth MR, Linstedt AD (2011) Structure of the membrane-tethering GRASP domain reveals a unique PDZ ligand interaction that mediates Golgi biogenesis. J Biol Chem 286(23):20125–20129. doi: 10.1074/jbc.C111.245324 |
Uversky VN (2009) Intrinsically disordered proteins and their environment: Effects of strong denaturants, temperate pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding. Protein J 28:305–325. doi: 10.1007/s10939-009-9201-4 |
van der Lee R, Buljan M, Lang B, Weatheritt RJ et al (2014) Classification of intrinsically disordered regions and proteins. Chem Rev 114(13):6589–6631. doi: 10.1021/cr400525m |
Wada A (1976) The alpha-helix as an electric macro-dipole. Adv Biophys:1–63 |
Wallace BA (2000) Conformational changes by synchrotron radiation circular dichroism spectroscopy. Nat Struct Biol 7(9):708–709. doi: 10.1038/78915 |
Wallace BA, Wien F, Miles AJ, Lees JG, Hoffmann SV, Evans P, Wistow GJ, Slingsby C (2004) Biomedical applications of synchrotron radiation circular dichroism spectroscopy: Identification of mutant proteins associated with disease and development of a reference database for fold motifs. Faraday Discuss 126:237–243 |
Wallace BA (2009) Protein characterisation by synchrotron radiation circular dichroism spectroscopy. Q Rev Biophys 42(4):317–370. doi: 10.1017/S003358351000003X |
Wallace BA, Janes RW (eds) (2009) Modern techniques for circular dichroism and synchrotron radiation circular dichroism spectroscopy. Advances in biomedical spectroscopy, vol 1. IOS Press, Amsterdam |
Whitmore L, Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32(Web Server issue):W668–73. |
Yoneda JS, Miles AJ, Araujo APU, Wallace BA (2017) Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation. Protein Sci 26(4):718726. doi: 10.1002/pro.3118 |