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1erf

From Proteopedia

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[[Image:1erf.gif|left|200px]]
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{{STRUCTURE_1erf| PDB=1erf | SCENE= }}
{{STRUCTURE_1erf| PDB=1erf | SCENE= }}
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'''CONFORMATIONAL MAPPING OF THE N-TERMINAL FUSION PEPTIDE OF HIV-1 GP41 USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)'''
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===CONFORMATIONAL MAPPING OF THE N-TERMINAL FUSION PEPTIDE OF HIV-1 GP41 USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)===
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==Overview==
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The N-terminal domain of HIV-1 glycoprotein 41000 (FP; residues 1--23; AVGIGALFLGFLGAAGSTMGARSCONH(2)) participates in fusion processes underlying virus--cell infection. Here, we use physical techniques to study the secondary conformation of synthetic FP in aqueous, structure-promoting, lipid and biomembrane environments. Circular dichroism and conventional, (12)C-Fourier transform infrared (FTIR) spectroscopy indicated the following alpha-helical levels for FP in 1-palmitoyl-2-oleoylphosphatidylglycerol (POPG) liposomes-hexafluoroisopropanol (HFIP)&gt;trifluoroethanol (TFE)&gt;phosphate-buffered saline (PBS). (12)C-FTIR spectra also showed disordered FP structures in these environments, along with substantial beta-structures for FP in TFE or PBS. In further experiments designed to map secondary conformations to specific residues, isotope-enhanced FTIR spectroscopy was performed using a suite of FP peptides labeled with (13)C-carbonyl at multiple sites. Combining these (13)C-enhanced FTIR results with molecular simulations indicated the following model for FP in HFIP: alpha-helix (residues 3-16) and random and beta-structures (residues 1-2 and residues 17-23). Additional (13)C-FTIR analysis indicated a similar conformation for FP in POPG at low peptide loading, except that the alpha-helix extends over residues 1-16. At low peptide loading in either human erythrocyte ghosts or lipid extracts from ghosts, (13)C-FTIR spectroscopy showed alpha-helical conformations for the central core of FP (residues 5-15); on the other hand, at high peptide loading in ghosts or lipid extracts, the central core of FP assumed an antiparallel beta-structure. FP at low loading in ghosts probably inserts deeply as an alpha-helix into the hydrophobic membrane bilayer, while at higher loading FP primarily associates with ghosts as an aqueous-accessible, beta-sheet. In future studies, (13)C-FTIR spectroscopy may yield residue-specific conformations for other membrane-bound proteins or peptides, which have been difficult to analyze with more standard methodologies.
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(as it appears on PubMed at http://www.pubmed.gov), where 11853678 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11853678}}
==About this Structure==
==About this Structure==
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[[Category: Gp41]]
[[Category: Gp41]]
[[Category: Viral fusion peptide]]
[[Category: Viral fusion peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:26:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:45:31 2008''

Revision as of 22:45, 30 June 2008

Image:1erf.png

Template:STRUCTURE 1erf

CONFORMATIONAL MAPPING OF THE N-TERMINAL FUSION PEPTIDE OF HIV-1 GP41 USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)

Template:ABSTRACT PUBMED 11853678

About this Structure

1ERF is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using (13)C-enhanced Fourier transform infrared spectroscopy., Gordon LM, Mobley PW, Pilpa R, Sherman MA, Waring AJ, Biochim Biophys Acta. 2002 Feb 15;1559(2):96-120. PMID:11853678

Page seeded by OCA on Tue Jul 1 01:45:31 2008

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