Related ArticlesHelix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and TFE solutions: 2D-1H NMR and CD studies in alanine-lysine peptides.
Biochemistry. 1998 Dec 8;37(49):17318-30
Authors: Padmanabhan S, Jiménez MA, Laurents DV, Rico M
Interactions between side chains spaced (i,i + 3) and (i,i + 4) may explain the context dependence of helix propensities observed in different systems. Nonpolar residues with these spacings occur frequently in protein helices and stabilize isolated peptide helices. Here (i,i + 3) and (i,i + 4) nonpolar interactions between Tyr and Leu in different solution conditions are studied in detail in alanine-based peptides using 2D 1H NMR and CD spectroscopy. Helix contents analyzed using current models for helix-coil transitions yield interaction energies which demonstrate significant helix stabilization in aqueous 1 M NaCl solutions by Tyr-Leu or Leu-Tyr pairs when spaced (i,i + 4) and, to a smaller extent, when spaced (i,i + 3), comparable to those estimated for other residue pairs. The interactions persist in solutions containing TFE, a helix-stabilizing solvent believed to diminish hydrophobic interactions, but not in helix-destabilizing 6 M urea. 1H NMR resonances for all peptides and solution conditions except in 6 M urea were completely assigned. NMR data indicate that the N-terminal residues are more helical and that the N-acetyl group participates in helix formation. The two (i,i + 4) spaced pairs show the same pattern of NOE cross-peaks between the Tyr and Leu side chains, as do the two (i,i + 3) pairs in 1 M NaCl as well in TFE solutions, and correspond well with that expected for the specific Tyr-Leu pair with side-chain contacts in protein helices.
[NMR paper] NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformation
NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
Related Articles NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
J Biol Chem. 2004 Aug 13;279(33):34963-70
Authors: Santiveri CM, Pérez-Cañadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M
The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy....
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[NMR paper] Solid-state NMR data support a helix-loop-helix structural model for the N-terminal h
Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form.
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J Mol Biol. 2001 Nov 2;313(4):845-59
Authors: Blanco FJ, Hess S, Pannell LK, Rizzo NW, Tycko R
Rev is a 116 residue basic protein encoded by the genome of human immunodeficiency virus type 1 (HIV-1) that binds to multiple sites in the Rev response element (RRE) of viral mRNA transcripts in...
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[NMR paper] The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
Biochemistry. 1997 Nov 4;36(44):13657-66
Authors: Wang G, Sparrow JT, Cushley RJ
The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments....
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[NMR paper] Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: k
Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and NMR studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and NMR studies.
FEBS Lett. 1995 Oct 30;374(2):165-8
Authors: Monasterio O, Nova E, López-Brauet A, Lagos R
The use of 3-fluoro-tyrosine as an alternative substrate for the enzyme tubulin:tyrosine ligase which catalyzes the...
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[NMR paper] PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, w
PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study.
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Biochemistry. 1995 Sep 12;34(36):11617-24
Authors: Chupin V, Killian JA, Breg J, de Jongh HH, Boelens R, Kaptein R, de Kruijff B
Proteins that are destined for export out of the cytoplasm of Escherichia coli cells are...
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[NMR paper] Measuring enzyme hydration in nonpolar organic solvents using NMR.
Measuring enzyme hydration in nonpolar organic solvents using NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Measuring enzyme hydration in nonpolar organic solvents using NMR.
Biotechnol Bioeng. 1995 Jun 5;46(5):452-8
Authors: Parker MC, Moore BD, Blacker AJ
A very sensitive NMR method has been developed for measuring deuterated water bound to proteins suspended in nonpolar solvents. This has been used to determine the amount of...
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[NMR paper] Determination of helix-helix interactions in membranes by rotational resonance NMR.
Determination of helix-helix interactions in membranes by rotational resonance NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Determination of helix-helix interactions in membranes by rotational resonance NMR.
Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):488-91
Authors: Smith SO, Bormann BJ
Dimerization of human glycophorin A in erythrocyte membranes is mediated by specific interactions within the helical transmembrane domain of the protein. Rotational...
Helix-stabilizing nonpolar interactions between tyrosine and leucine in aqueous and T
Linear Mode
