About: The influence of proline residues on alpha-helical structure

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About: The influence of proline residues on alpha-helical structure Goto Sponge NotDistinct Permalink

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scientific article published on 01 December 1990

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 1990 (uk) article scientifique publié en 1990 (fr) im Dezember 1990 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'avientu de 1990 (ast) գիտական հոդված հրատարակված 1990 թվականի դեկտեմբերի 1-ին (hy) scientific article published on 01 December 1990 (en)
publication date	wds:Q68646142-2E52C193-0257-4EC8-B5A0-5F42DCC35B8D
publication date	1990-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q68646142-E03EDB0B-5F71-41FF-AFD5-C247A1508DA0
language of work or name	English
cites work	wds:Q68646142-0A4C15A2-C2E3-4B92-AFBF-4563F4A99116 wds:Q68646142-0B4B1900-18DC-4CDB-B633-2C3A064F4674 wds:Q68646142-17B44D0C-FB7B-4F92-B38C-2869172CC0C8 wds:Q68646142-226578B2-0EAC-4E76-A6AD-C205FD04A85B wds:Q68646142-49DA2758-3155-469F-993D-DE3C5B4D6863 wds:Q68646142-632158FF-378C-48A0-83DE-5093EA263B51 wds:Q68646142-73C55099-5AAB-4197-8534-CF76D641683A wds:Q68646142-9AD565E8-4BEB-4869-8898-D65DAB5E659A wds:Q68646142-9D6ABE81-A936-4E7D-894C-FB96CD7A3F2B wds:Q68646142-A7B20200-9E97-4744-9F69-16AD513EC668 wds:Q68646142-AF94C6FC-7471-466E-AD15-3301C75A9ECF wds:Q68646142-CDD0162E-A334-49E3-9F2F-8E5F51D061ED wds:Q68646142-DBD5963F-9E00-4CC4-815B-079747D3F533 wds:Q68646142-DF516C93-A1C0-4B67-A777-3DDB7F5008A9 wds:Q68646142-ED6DF9F5-6A9F-4D47-BF6E-F8DAC918E118 wds:Q68646142-F682343D-FB10-4532-9821-CEEDE5BD3747
cites work	Amino acid preferences for specific locations at the ends of alpha helices The helical hydrophobic moment: a measure of the amphiphilicity of a helix Helix signals in proteins The interpretation of protein structures: Estimation of static accessibility Use of helical wheels to represent the structures of proteins and to identify segments with helical potential The structure of melittin in membranes Surface and inside volumes in globular proteins A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution Helix geometry in proteins Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins Structural invariants in protein folding Capping and alpha-helix stability Hypothesis about the function of membrane-buried proline residues in transport proteins Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds The structure of melittin. A 1H-NMR study in methanol Solvent-induced distortions and the curvature of alpha-helices
author name string	wds:Q68646142-1EBFF65C-4A17-4937-9A8A-A7933E178309 wds:Q68646142-F1FC887B-3F1E-402A-9DC3-B357BAAD1CBD
author name string	Williams DH Woolfson DN
rdfs:label	The influence of proline residues on alpha-helical structure (en) The influence of proline residues on alpha-helical structure (nl)
skos:prefLabel	The influence of proline residues on alpha-helical structure (en) The influence of proline residues on alpha-helical structure (nl)
name	The influence of proline residues on alpha-helical structure (en) The influence of proline residues on alpha-helical structure (nl)
title	wds:Q68646142-9DD58422-240A-445B-B0D0-B512F62120B5
title	The influence of proline residues on alpha-helical structure (en)
page(s)	wds:Q68646142-D2B181C9-AF7A-46D5-BC95-B25B534A6DDE
page(s)	185-188
instance of	wds:Q68646142-565472CE-CB1A-4440-A57C-65AE96B4B8F2
instance of	scholarly article
PubMed ID	wds:Q68646142-D2DEC57B-9CC2-4C30-BA6F-531DC0146A97
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2269352
PubMed ID	2269352
published in	wds:Q68646142-375BC722-28DF-49E7-BA91-D035273749E6
published in	FEBS Letters
issue	wds:Q68646142-4F9D0119-BE3A-41AE-AB49-52C1C6E32A23
volume	wds:Q68646142-79196DEC-15E7-41EC-BBFE-9FF107DDEEFC
issue	1-2
volume	277
DOI	wds:Q68646142-F3FE4D23-3E37-4C75-BCA7-B84A277DC3E4
DOI	http://dx.doi.org/10.1016/0014-5793(90)80839-B
DOI	10.1016/0014-5793(90)80839-B
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68646142
is cites work of	A mutation in C2orf64 causes impaired cytochrome c oxidase assembly and mitochondrial cardiomyopathy Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity Dissecting the functions of conserved prolines within transmembrane helices of the D2 dopamine receptor. Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains The properties of ion channels formed by zervamicins Helix D elongation and allosteric activation of antithrombin. Geometrical and sequence characteristics of alpha-helices in globular proteins CSE1 and CSE2, two new genes required for accurate mitotic chromosome segregation in Saccharomyces cerevisiae The TXP motif in the second transmembrane helix of CCR5. A structural determinant of chemokine-induced activation The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions The LZT proteins; the LIV-1 subfamily of zinc transporters On the use of the transmembrane domain of bacteriorhodopsin as a template for modeling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors The biophysics of peptide models of ion channels Proline in α-helical kink is required for folding kinetics but not for kinked structure, function, or stability of heat shock transcription factor Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment The role of proline and glycine in determining the backbone flexibility of a channel-forming peptide Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin Predicting oligomerization states of coiled coils New insights into the spring-loaded conformational change of influenza virus hemagglutinin The mat- allele of Podospora anserina contains three regulatory genes required for the development of fertilized female organs. Proline-induced distortions of transmembrane helices. Identification of proline residues in or near the transmembrane helices of the human breast cancer resistance protein (BCRP/ABCG2) that are important for transport activity and substrate specificity The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors Role of conserved prolines in the structure and function of the Na+/dicarboxylate cotransporter 1, NaDC1. Conformational flexibility of helix VI is essential for substrate permeation of the human apical sodium-dependent bile acid transporter Peptide Self-Replication Enhanced by a Proline Kink Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 ORF50/Rta lytic switch protein functions as a tetramer

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