메뉴 건너뛰기




Volumn 33, Issue SUPPL. 2, 1998, Pages 22-27

Stability of secondary structural elements in a solvent-free environment. II: The β-pleated sheets

Author keywords

pleated sheet; Electrostatic interactions; Hydrogen bonds; Mass spectrometry; Molecular mechanics calculations; Secondary structure

Indexed keywords

BOMBESIN; POLYPEPTIDE; PEPTIDE; SOLVENT;

EID: 0032253728     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(1998)33:2+<22::AID-PROT4>3.0.CO;2-6     Document Type: Article
Times cited : (22)

References (33)
  • 2
    • 33748233229 scopus 로고    scopus 로고
    • Electrospray mass spectrometry of biomacromolecular complexes with noncovalent interactions - New analytical perspectives for supramolecular chemistry and molecular recognition processes
    • Przybylski, M., Glocker, M.O. Electrospray mass spectrometry of biomacromolecular complexes with noncovalent interactions - new analytical perspectives for supramolecular chemistry and molecular recognition processes. Angew. Chem. Int. Ed. Engl. 35:806-826, 1996.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 806-826
    • Przybylski, M.1    Glocker, M.O.2
  • 3
    • 37049070609 scopus 로고
    • Does the observation of non-covalent complexes between biomolecules by electrospray ionization mass spectrometry necessarily reflect specific solution interaction?
    • Aplin, R.T, Robinson, C.V., Schofield, C.J., Westwood, N.J. Does the observation of non-covalent complexes between biomolecules by electrospray ionization mass spectrometry necessarily reflect specific solution interaction? J. Chem. Soc. Chem. Comm. 1994:2415-2417, 1994.
    • (1994) J. Chem. Soc. Chem. Comm. , vol.1994 , pp. 2415-2417
    • Aplin, R.T.1    Robinson, C.V.2    Schofield, C.J.3    Westwood, N.J.4
  • 4
    • 0030626588 scopus 로고    scopus 로고
    • The Levinthal paradox: Yesterday and today
    • Karplus, M. The Levinthal paradox: Yesterday and today. Fold. Des. 2:S69-S75, 1997.
    • (1997) Fold. Des. , vol.2
    • Karplus, M.1
  • 5
    • 0031052179 scopus 로고    scopus 로고
    • Protein structure: What is it possible to predict now?
    • Finkelstein, A.V. Protein structure: What is it possible to predict now? Curr. Opin. Struct. Biol. 7:60-71, 1997.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 60-71
    • Finkelstein, A.V.1
  • 6
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A., Chan, H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19, 1997.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 7
    • 0027236794 scopus 로고
    • Structural basis for amino acid α-helix propensity
    • Blaber, M., Zhang, X., Matthews, B. Structural basis for amino acid α-helix propensity. Science 260:1637-1640, 1993.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.2    Matthews, B.3
  • 8
    • 0030057864 scopus 로고    scopus 로고
    • What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties
    • Munson, M., Balasubramanian, S., Fleming, K.G. et al. What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Protein Sci. 5:1584-1593, 1996.
    • (1996) Protein Sci. , vol.5 , pp. 1584-1593
    • Munson, M.1    Balasubramanian, S.2    Fleming, K.G.3
  • 9
    • 0031038377 scopus 로고    scopus 로고
    • Local interactions in protein folding: Lessons from the α-helix
    • Aurora, R., Creamer, T.P., Srinivasan, R., Rose, G.D. Local interactions in protein folding: Lessons from the α-helix. J. Biol. Chem. 272:1413-1416, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1413-1416
    • Aurora, R.1    Creamer, T.P.2    Srinivasan, R.3    Rose, G.D.4
  • 10
    • 0028960071 scopus 로고
    • Role of screening in determining protein main chain conformational preferences
    • Avbelj, F., Moult, J. Role of screening in determining protein main chain conformational preferences. Biochemistry 34:755-764, 1995.
    • (1995) Biochemistry , vol.34 , pp. 755-764
    • Avbelj, F.1    Moult, J.2
  • 11
    • 0026608073 scopus 로고
    • Environment affects amino acid preference for secondary structure
    • Zhong, L., Jonson, W.C. Environment affects amino acid preference for secondary structure. Proc. Natl. Acad. Sci. U.S.A. 89:4462-4465, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4462-4465
    • Zhong, L.1    Jonson, W.C.2
  • 12
    • 0029588554 scopus 로고
    • High helical propensity of the peptide from β-lactoglobulin, a predominantly β-sheet protein
    • Hamada, D., Kuroda, Y., Tanaka, T., Goto, Y. High helical propensity of the peptide from β-lactoglobulin, a predominantly β-sheet protein. J. Mol. Biol. 254:737-746, 1995.
    • (1995) J. Mol. Biol. , vol.254 , pp. 737-746
    • Hamada, D.1    Kuroda, Y.2    Tanaka, T.3    Goto, Y.4
  • 13
    • 0030342681 scopus 로고    scopus 로고
    • Conformational switching in designed peptides: The helix/sheet transition
    • Cepra, R., Cohen, F.E., Kuntz, I.D. Conformational switching in designed peptides: the helix/sheet transition. Fold. Des. 1:91-101, 1996.
    • (1996) Fold. Des. , vol.1 , pp. 91-101
    • Cepra, R.1    Cohen, F.E.2    Kuntz, I.D.3
  • 14
    • 0029664917 scopus 로고    scopus 로고
    • 12+ ions produced by electrospray ionization mass spectrometry
    • 12+ ions produced by electrospray ionization mass spectrometry. J. Mass Spectrom. 31:247-254, 1996.
    • (1996) J. Mass Spectrom. , vol.31 , pp. 247-254
    • Cassady, C.J.1    Carr, S.R.2
  • 15
    • 0030905633 scopus 로고    scopus 로고
    • Ion mobility measurements and their applications to clusters and biomolecules
    • Clemmer, D.E., Jarrold, M.F. Ion mobility measurements and their applications to clusters and biomolecules. J. Mass Spectrom. 32:577-592, 1997.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 577-592
    • Clemmer, D.E.1    Jarrold, M.F.2
  • 18
    • 0028803925 scopus 로고
    • A direct comparison of the "first" and "second" gas phase basicities of an octapeptide RPPGFSPF
    • Kaltashov, I.A., Fenselau, C. A direct comparison of the "first" and "second" gas phase basicities of an octapeptide RPPGFSPF. J. Am. Chem. Soc. 117:9906-9910, 1995.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9906-9910
    • Kaltashov, I.A.1    Fenselau, C.2
  • 19
    • 0029933305 scopus 로고    scopus 로고
    • The importance of charge-separation reactions in tandem mass spectrometry of doubly protonated angiotensin II formed by electrospray ionization: Experimental considerations and structural implications
    • Adams, J., Strobel, F., Reiter, A., Sullards, M.C. The importance of charge-separation reactions in tandem mass spectrometry of doubly protonated angiotensin II formed by electrospray ionization: Experimental considerations and structural implications. J. Am. Soc. Mass Spectrom. 7:30-41, 1996.
    • (1996) J. Am. Soc. Mass Spectrom. , vol.7 , pp. 30-41
    • Adams, J.1    Strobel, F.2    Reiter, A.3    Sullards, M.C.4
  • 20
    • 0030845114 scopus 로고    scopus 로고
    • Conformation of doubly protonated peptides studied by charge-separation reactions in mass spectrometry
    • Szilagyi, Z., Drahos, L., Vekey, K. Conformation of doubly protonated peptides studied by charge-separation reactions in mass spectrometry. J. Mass Spectrom. 32:689-696. 1997.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 689-696
    • Szilagyi, Z.1    Drahos, L.2    Vekey, K.3
  • 21
    • 0031056524 scopus 로고    scopus 로고
    • Stability of secondary structural elements in a solvent-free environment: The α-helix
    • Kaltashov, I.A., Fenselau, C. Stability of secondary structural elements in a solvent-free environment: The α-helix. Proteins 27:166-171, 1997.
    • (1997) Proteins , vol.27 , pp. 166-171
    • Kaltashov, I.A.1    Fenselau, C.2
  • 22
    • 84989084967 scopus 로고
    • Calculation of the kinetic energy release of charge separation processes
    • Vekey, K., Pocsfalvi, G. Calculation of the kinetic energy release of charge separation processes. Org. Mass Spectrom. 27:1203-1209, 1992.
    • (1992) Org. Mass Spectrom. , vol.27 , pp. 1203-1209
    • Vekey, K.1    Pocsfalvi, G.2
  • 24
    • 0020991935 scopus 로고
    • Structural properties of protein β-sheets
    • Salemme, F.R. Structural properties of protein β-sheets. Prog. Biophys. Mol. Biol. 42:95-133, 1983.
    • (1983) Prog. Biophys. Mol. Biol. , vol.42 , pp. 95-133
    • Salemme, F.R.1
  • 26
  • 27
    • 0023804303 scopus 로고
    • Contributions of mass spectrometry to peptide and protein structure
    • Biemann, K. Contributions of mass spectrometry to peptide and protein structure. Biomed. Environ. Mass Spectrom. 16:99-111, 1988.
    • (1988) Biomed. Environ. Mass Spectrom. , vol.16 , pp. 99-111
    • Biemann, K.1
  • 28
    • 0028796485 scopus 로고
    • Conformational structure of bombesin studied by vibrational and circular dichroism spectroscopy
    • Carmona, P., Lasagabaster, A., Molina, M. Conformational structure of bombesin studied by vibrational and circular dichroism spectroscopy. Biochim. Biophys. Acta 1246:128-134, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1246 , pp. 128-134
    • Carmona, P.1    Lasagabaster, A.2    Molina, M.3
  • 29
    • 0001117058 scopus 로고    scopus 로고
    • Construction and design of β-sheets
    • Smith, C.K., Regan, L. Construction and design of β-sheets. Accts. Chem. Res. 30:153-161, 1997.
    • (1997) Accts. Chem. Res. , vol.30 , pp. 153-161
    • Smith, C.K.1    Regan, L.2
  • 30
    • 0029891313 scopus 로고    scopus 로고
    • De novo design and structural analysis of a model β-hairpin peptide system
    • Ramirez-Alvarado, M., Blanco, F.J., Serrano, L. De novo design and structural analysis of a model β-hairpin peptide system. Nat. Struct. Biol. 3:604-612, 1996.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 604-612
    • Ramirez-Alvarado, M.1    Blanco, F.J.2    Serrano, L.3
  • 31
    • 84990637902 scopus 로고
    • Proton affinity of arginine measured by the kinetic approach
    • Wu, Z., Fenselau, C. Proton affinity of arginine measured by the kinetic approach. Rapid Comm. Mass Spectrom. 6:403-405, 1992.
    • (1992) Rapid Comm. Mass Spectrom. , vol.6 , pp. 403-405
    • Wu, Z.1    Fenselau, C.2
  • 32
    • 84990637897 scopus 로고
    • Gas phase basicities and proton affinities of lysine and histidine measured from the dissociation of proton-bound dimers
    • Wu, Z., Fenselau, C. Gas phase basicities and proton affinities of lysine and histidine measured from the dissociation of proton-bound dimers. Rapid Comm. Mass Spectrom. 9:777-780, 1994.
    • (1994) Rapid Comm. Mass Spectrom. , vol.9 , pp. 777-780
    • Wu, Z.1    Fenselau, C.2
  • 33
    • 0030941296 scopus 로고    scopus 로고
    • NMR structure of a de novo designed peptide 33mer with two distinct compact β-sheet folds
    • Ilyina, E., Roongta, V., Mayo, K.H. NMR structure of a de novo designed peptide 33mer with two distinct compact β-sheet folds. Biochemistry 36:5245-5250, 1997.
    • (1997) Biochemistry , vol.36 , pp. 5245-5250
    • Ilyina, E.1    Roongta, V.2    Mayo, K.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.