The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix (Q27731318)

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English	The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix	scientific article

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title

The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix (English)

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author

Kurt Wüthrich

series ordinal

4

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Thomas Szyperski

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2

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Jan Johansson

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1

object named as

J Johansson

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author name string

T Curstedt

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3

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language of work or name

English

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publication date

17 May 1994

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published in

Biochemistry

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volume

33

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issue

19

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page(s)

6015-23

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cites work

Interaction of lipid vesicles with monomolecular layers containing lung surfactant proteins SP-B or SP-C.

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Nucleotide and amino acid sequences of pulmonary surfactant protein SP 18 and evidence for cooperation between SP 18 and SP 28-36 in surfactant lipid adsorption

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Interaction between perdeuterated dimyristoylphosphatidylcholine and low molecular weight pulmonary surfactant protein SP-C

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Support of1H NMR assignments in proteins by biosynthetically directed fractional13C-labeling

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Structure and orientation of the surfactant-associated protein C in a lipid bilayer

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The proteins of the surfactant system

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Structure determination of the Antp(C39 → S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA

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1H And 13C NMR chemical shifts of the diastereotopic methyl groups of valyl and leucyl residues in peptides and proteins

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Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA

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Two hydrophobic low-molecular-mass protein fractions of pulmonary surfactant. Characterization and biophysical activity

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Protein folding by restrained energy minimization and molecular dynamics

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

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Size and structure of the hydrophobic low molecular weight surfactant-associated polypeptide

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Effects of lung surfactant proteolipid SP-C on the organization of model membrane lipids: a fluorescence study

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Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.

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Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylcholine bilayers: differential scanning calorimetric and FTIR spectroscopic studies

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Conformational preferences of amino acids in globular proteins

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Characterization of lipid insertion into monomolecular layers mediated by lung surfactant proteins SP-B and SP-C

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Hydrophobic 3.7 kDa surfactant polypeptide: Structural characterization of the human and bovine forms

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Prediction of protein conformation

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Lipid effects on aggregation of pulmonary surfactant protein SP-C studied by fluorescence energy transfer

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A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

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IUPAC-IUB Commission on Biochemical Nomenclature. Abbreviations and symbols for the description of the conformation of polypeptide chains. Tentative rules (1969)

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Topogenic signals in integral membrane proteins

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Analysis of the palmitoylation and membrane targeting domain of neuromodulin (GAP-43) by site-specific mutagenesis

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Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

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Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups

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Conformations of poly-L-valine in solution

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An all atom force field for simulations of proteins and nucleic acids

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2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-sn-glycero-3-phosphocholine headgroup: a model for transbilayer peptides in surfactant and biological membranes

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Efficient analysis of protein 2D NMR spectra using the software packageEASY

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Structure and functions of a dimeric form of surfactant protein SP-C: a Fourier transform infrared and surfactometry study

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Role of bovine pulmonary surfactant-associated proteins in the surface-active property of phospholipid mixtures

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Canine hydrophobic surfactant polypeptide SP-C. A lipopeptide with one thioester-linked palmitoyl group

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Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids

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Processing of multi-dimensional NMR data with the new software PROSA

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10.1021/BI00185A042

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2170547

OpenCitations bibliographic resource ID

2170547

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2170547

The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix (Q27731318)

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The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix (Q27731318)

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