Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals.
about
Prevalence and nonrandom distribution of exonic mutations in interferon regulatory factor 6 in 307 families with Van der Woude syndrome and 37 families with popliteal pterygium syndromeMissense mutations that cause Van der Woude syndrome and popliteal pterygium syndrome affect the DNA-binding and transcriptional activation functions of IRF6Computational Design of Thermostabilizing d -Amino Acid SubstitutionsAcrB trimer stability and efflux activity, insight from mutagenesis studiesReverse engineering the (beta/alpha )8 barrel fold.Cotranslational incorporation of a structurally diverse series of proline analogues in an Escherichia coli expression system.SDS, a structural disruption score for assessment of missense variant deleteriousness.Structures, basins, and energies: a deconstruction of the Protein Coil Library.pi-Turns: types, systematics and the context of their occurrence in protein structures.Mapping side chain interactions at protein helix termini.Folding by numbers: primary sequence statistics and their use in studying protein foldingAmino acid alphabet reduction preserves fold information contained in contact interactions in proteins.Asparagine and glutamine differ in their propensities to form specific side chain-backbone hydrogen bonded motifs in proteins.Phosphorylation of paxillin LD4 destabilizes helix formation and inhibits binding to focal adhesion kinase.Designing human m1 muscarinic receptor-targeted hydrophobic eigenmode matched peptides as functional modulatorsThe role of alpha-, 3(10)-, and pi-helix in helix-->coil transitions.An allelic series of mutations in the kit ligand gene of mice. I. Identification of point mutations in seven ethylnitrosourea-induced Kitl(Steel) alleles.Mutation analysis of the Pip interaction domain reveals critical residues for protein-protein interactions.De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains.Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxinThe exceptionally high reactivity of Cys 621 is critical for electrophilic activation of the sensory nerve ion channel TRPA1.A novel secondary structure based on fused five-membered rings motifCoiled coils and SAH domains in cytoskeletal molecular motors.The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins.OGlcNAcylation and phosphorylation have similar structural effects in α-helices: post-translational modifications as inducible start and stop signals in α-helices, with greater structural effects on threonine modification.Experimental and Computational Analysis of Protein Stabilization by Gly-to-d-Ala Substitution: A Convolution of Native State and Unfolded State Effects.Analysis of residue conformations in peptides in Cambridge structural database and protein-peptide structural complexes.Computational Biology and Bioinformatics: a tinge of Indian spice.Pore mutations of the Escherichia coli MscS channel affect desensitization but not ionic preference.Molecular carpentry: piecing together helices and hairpins in designed peptides.Effects of hydrogen-bond deletion on peptide helices: structural characterization of depsipeptides containing lactic acid.Influence of solvent molecules on the stereochemical code of glycyl residues in proteins.Context-dependent effects of proline residues on the stability and folding pathway of ubiquitin.The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.The most C-terminal tri-glycine segment within the polyglycine stretch of the pea Toc75 transit peptide plays a critical role for targeting the protein to the chloroplast outer envelope membrane.Comprehensive analysis of the helix-X-helix motif in soluble proteins.Characteristics of a PHD Finger Subtype.Phylogenetic sequence analysis and functional studies reveal compensatory amino acid substitutions in loop 2 of human ribonucleotide reductase.Water and side-chain embedded π-turns.The duplication of an eight-residue helical stretch in Staphylococcal nuclease is not helical: a model for evolutionary change.
P2860
Q24645286-616C90EC-E84A-4F58-8CCB-2AE16F7F8697Q24655503-BA024B89-F4BA-4597-ABBF-75DD3C3161CEQ27674761-4F3AD85C-A77F-4BEE-8F5D-8EE79353D06FQ28478270-3C3352D5-EDF6-4518-9B9C-E20D754344FDQ30168406-96210260-3178-49FF-8A2D-47116ADA5A7DQ30342165-FC25ED80-518D-45FA-B6F1-F03F560460E0Q30362211-D0DB44C9-8286-4271-BD6E-758D14B0D417Q30369034-DF949F03-B635-4D2A-8BBC-378962E43DD2Q30372205-1BB62BBB-7BFB-4B09-96AE-A3F8E15BB5E6Q30377151-DB4720EC-9D6B-4DAA-B17E-E384021BD9D0Q30377510-1A5E077E-FE1E-41B7-A32A-15BB1C571A7EQ30379551-E6B12284-9EF5-4F34-A4FF-C3670F938C21Q30411473-9876ADAA-FC00-49EE-B6BC-65CEA5FA8F2FQ33744698-0DF9A437-FCB5-49EA-9B5B-03C775F41DAFQ34184921-51B1DEA7-D73D-4478-AC1A-0B47CE31A590Q34199126-0D805F6D-9D90-4658-BFB7-0DC8BE631098Q34615833-E11AC66A-89B1-488B-9ED4-8B9218CCE6CBQ35059830-AA898344-6972-4A69-A6F5-96D30D26CCDAQ35103478-732408D0-84C7-4EFF-8A23-673B0F4843DDQ36281341-90BBF7BF-AA9E-4233-84DB-C46FF4D7B095Q36949699-9B46D84F-C8AC-43D2-BBD7-9F551576C5A9Q37166548-3072E811-2BF6-472B-98F6-4D2E515907E1Q37936477-DD38D9E2-F5D1-4A02-AC7A-87A59CB0A2AFQ38779767-EEB52088-FACB-4C7E-82CA-D9A788CE7B6CQ39045464-268C5178-6210-431F-9294-DB922D8135B8Q39116654-18E098E4-AABF-47A3-BB9E-4D42EA7FA739Q39428214-2A4A03B2-E5E0-4F56-8804-A5DD9F6763BCQ42734741-3527A699-04F8-43FE-88E1-EFBF73971E37Q43088410-C16CD5AD-BC40-4EA4-B5EF-A6CB1FCBD5A0Q43566012-BAB866A7-9F77-4E26-B9A0-6345DCDD6F5DQ43688057-A13D67E8-7F60-4E57-8448-D62A2C6D7977Q44165213-31FDB93E-6A1B-49E5-8F6E-05EA12631D2BQ45160533-79F1E430-3DC1-4EDC-B92A-8B066CAB7AE3Q45258108-3F9645A1-D712-4B2C-AD49-CDF986F12CCCQ46159899-9E749B7C-3890-46B5-AF31-0365C2B2AB98Q46794984-8227A3F7-B99D-4B45-979A-5A61D3A12B8DQ47281158-30200DE5-7C3F-44AA-B644-0E39F2C2F681Q47952981-523A5708-2239-4EF0-BB8B-2FD737371367Q48431415-A505D7EE-A7DD-4C1A-AF52-7F39962D76BAQ52077265-C94E640D-8A63-4F11-9448-E9E446197B20
P2860
Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals.
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Stereochemical punctuation mar ...... containing helix stop signals.
@ast
Stereochemical punctuation mar ...... containing helix stop signals.
@en
Stereochemical punctuation mar ...... containing helix stop signals.
@nl
type
label
Stereochemical punctuation mar ...... containing helix stop signals.
@ast
Stereochemical punctuation mar ...... containing helix stop signals.
@en
Stereochemical punctuation mar ...... containing helix stop signals.
@nl
prefLabel
Stereochemical punctuation mar ...... containing helix stop signals.
@ast
Stereochemical punctuation mar ...... containing helix stop signals.
@en
Stereochemical punctuation mar ...... containing helix stop signals.
@nl
P2093
P356
P1476
Stereochemical punctuation mar ...... containing helix stop signals.
@en
P2093
Gunasekaran K
Nagarajaram HA
Ramakrishnan C
P304
P356
10.1006/JMBI.1997.1505
P407
P577
1998-02-01T00:00:00Z