The reverse turn as a polypeptide conformation in globular proteins. - Wikidata - awgldk - TriplyDB

The reverse turn as a polypeptide conformation in globular proteins.

The reverse turn as a polypeptide conformation in globular proteins.

http://www.wikidata.org/entity/Q35096739

about

The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution PDBparam: Online Resource for Computing Structural Parameters of Proteins The Three-Dimensional Structure of Bovine Calcium Ion-Bound Osteocalcin Using 1HNMR Spectroscopy Intramolecularly hydrogen-bonded peptide conformations Knowledge-Based Protein Modeling Analysis of physicochemical and structural properties determining HIV-1 coreceptor usage Molecular evolution of alcohol dehydrogenase 1 in members of the grass family Folding patterns of porin and bacteriorhodopsin.A Rough Set-Based Model of HIV-1 Reverse Transcriptase Resistome Water mediation is essential to nucleation of β-turn formation in peptide folding motifs.Computational Analysis of Molecular Interaction Networks Underlying Change of HIV-1 Resistance to Selected Reverse Transcriptase Inhibitors.Amino acid sequence preferences to control cell-specific organization of endothelial cells, smooth muscle cells, and fibroblasts.Gramicidin D conformation, dynamics and membrane ion transport.Mutations around the NG59 lesion indicate an active association of polyoma virus middle-T antigen with pp60c-src is required for cell transformation.Heterodimer formation and crystal nucleation of gramicidin D.Prediction of beta-turns.Conformation of somatostatin using scalar coupling constants from 270 and 600 MHz simulated proton magnetic resonance spectra Analysing the substrate multispecificity of a proton-coupled oligopeptide transporter using a dipeptide library.Theoretical studies on pro-leu-gly-nh2 conformation.Identification of beta,beta-turns and unordered conformations in polypeptide chains by vacuum ultraviolet circular dichroism.Local interactions in bends of proteins.Structural elements in the N-terminal half of transcription factor IIIA required for factor binding to the 5S RNA gene internal control region The (1)H NMR structure of bovine Pb(2+)-osteocalcin and implications for lead toxicity Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.Extension of the classical classification of β-turns.Vibrational analysis of peptides, polypeptides, and proteins: Characteristic amide bands of beta-turns.Amino acid sequence of tyrosinase from Neurospora crassa.Breaking the singleton of germination protease Structural and Mechanistic Implications of Rearrangement Frequencies within Human TCRBV Genes.An approach toward the determination of the tertiary structure of MS2 coat protein [proceedings]X-ray enzymology.Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature.Focused Screening of ECM-Selective Adhesion Peptides on Cellulose-Bound Peptide Microarrays.Amino acid distributions around O-linked glycosylation sites.Structural studies of the N-terminus of Connexin 32 using 1H NMR spectroscopy Structural studies of N-terminal mutants of connexin 32 using (1)H NMR spectroscopy.Analysis of the code relating sequence to conformation in globular proteins. An informational analysis of the role of the residue in determining the conformation of its neighbours in the primary sequence.Studies of triose phosphate isomerase by hydrogen exchange.Crystal structure analysis of amicyanin and apoamicyanin from Paracoccus denitrificans at 2.0 A and 1.8 A resolution

P2860

Q24540326-350221CF-952E-4B4B-BE27-294F19FE5C7C Q24564676-6FA9C242-B909-4FB1-8E7F-3CC201803DD9 Q26744061-605EA693-C281-4C32-8460-365A728110CA Q27641467-D95F9AFD-8D0B-45E4-8AF3-806BB7079481 Q28263768-A8BC37BE-7A25-44A5-B924-2CE47701CF17 Q28315523-F3B21BBA-ADD5-413D-BB6D-89A51E705BBE Q28488611-B44B02E4-8F75-4A15-B822-DD0BE1C39BEF Q28775819-8DB50C4B-290E-40EF-87A4-9C0C0B979B16 Q30403353-D78EC0DC-8721-4F64-BED9-E27234A3ED44 Q30492811-A76A4213-2B32-4F3A-8579-CBABB71868AA Q30678312-3673A029-2744-402F-B223-C5DB7014A3C9 Q33793189-FE205CD4-9AA4-46D5-BA43-1AC8A507169F Q33832534-6FEBDE40-9EB8-4FF5-9FC2-CB0826853E40 Q33867347-E13B6006-A02D-4873-B836-5A4D60CCEC0D Q33879388-18B24488-E518-4883-849C-D59D1ACB4926 Q34169251-29B440BA-74B4-43E6-9BA3-25D495F6D3A1 Q34254354-9975CF04-DC99-44E1-9F6D-1043F2041E35 Q34256499-9D88961A-5B70-43CD-AE88-F8B5FE311EAD Q34995844-E4D96F2A-A2ED-4662-B8EF-98FCD470AF69 Q34997060-39810871-EBEF-49A2-A32C-637AF466F8A9 Q35042033-73FB1AA0-8CE0-44D3-A8EA-23AA71A37985 Q35054985-93B552A1-58E8-457F-80E1-CE222313F869 Q35800928-004588BB-685C-44B9-84A8-2FAF300B3279 Q35897413-62239139-14E2-44C8-B264-9CB4A2C1653F Q36710757-3A06B760-A0C3-421A-A7E2-92E65EFF4E1F Q37257588-FE2E917E-0637-403E-BC3B-626475CB368F Q37315023-71DBF443-2F04-4095-94D5-B3A6C9C758DB Q37591812-0D3665B1-5D12-4518-B39B-F7B54FDA548C Q38269113-F323BDF7-C09D-4350-B63E-6CDC20B2BCF6 Q38703920-B2EC768C-F810-44E6-9B77-BCED5D96A41D Q39500102-073F6EE7-1848-48A1-9161-2DE7FE59A9DD Q40480285-DDDBFF81-FE57-4D1B-9C7E-89482A3FD211 Q41203584-EEE72433-AA24-4947-8655-8E374A7BC160 Q41704460-434BF421-AA36-4E1C-AC9F-2A821FC7E514 Q41761661-9611F067-1794-42DA-89AC-B96639C18D12 Q41762529-711FF51E-5402-46D5-9F98-C6926569A773 Q41892577-AA1E0A39-7447-41CE-BC8B-A5C31BFA5F04 Q41908902-1714F146-DECC-450C-B446-24C223A463A4 Q41909902-C87CF198-9FD3-4C2D-AB4C-4B635D200382 Q42200829-BA901023-F6F5-41C4-8361-1E0B1882F254

P2860

The reverse turn as a polypeptide conformation in globular proteins.

http://www.wikidata.org/entity/Q35096739

description

1973 nî lūn-bûn

@nan

1973 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1973 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

1973年の論文

@ja

1973年論文

@yue

1973年論文

@zh-hant

1973年論文

@zh-hk

1973年論文

@zh-mo

1973年論文

@zh-tw

1973年论文

@wuu

name

The reverse turn as a polypeptide conformation in globular proteins.

@ast

The reverse turn as a polypeptide conformation in globular proteins.

@en

type

label

The reverse turn as a polypeptide conformation in globular proteins.

@ast

The reverse turn as a polypeptide conformation in globular proteins.

@en

prefLabel

The reverse turn as a polypeptide conformation in globular proteins.

@ast

The reverse turn as a polypeptide conformation in globular proteins.

@en

P1433

Q35096739-F38BC6AC-8D84-4770-8BC9-8F62A0667680

P1476

Q35096739-50088FAF-B89F-460F-AFB2-1F8879B5D1DF

P2093

Q35096739-19509786-3715-4B58-9B67-1DD053C76399

Q35096739-1CB8EDB0-F663-4E89-B75A-79F641CBBEA4

Q35096739-52FF4C57-0F41-46D4-B5BC-463F8D448C90

P2860

Q35096739-06DE3E65-70BD-4EAB-BD4F-57253C9514A1

Q35096739-1085B967-BB7C-4EE2-A54E-8E47D239A226

Q35096739-28D7EB7A-ED31-4A48-905E-963610828CB4

Q35096739-2976F555-5E6E-496D-90C6-8E404F3632B2

Q35096739-50B7D544-8717-4A52-8755-A3E730F9BCA6

Q35096739-524742B3-E4FB-4CA0-82CD-ADC4623E5DB6

Q35096739-70BB1C67-39FF-4322-BFBA-F51AE0048715

Q35096739-E5EA746F-B7EB-40EE-B753-EE9A8E6368D4

P304

Q35096739-11BAAAD9-28BA-4875-8700-359FA1D5E6AE

P31

Q35096739-0F039DCC-7651-4040-B346-B0469CA5A803

P356

Q35096739-BA515B93-0CE7-4F14-9F30-112FD5657C28

P407

Q35096739-CA7BEE1D-AE32-4CE9-932E-590218A46422

P433

Q35096739-6AD23134-76BC-41B4-85E6-96D88A3542F5

P478

Q35096739-CC5A0D36-06FC-42F8-93FB-C56A999E3C10

P577

Q35096739-4D2D6553-F02C-4B01-8C38-49E87AEF29CC

P5875

Q35096739-179EF4B0-8ED8-4D2D-8302-CE47348AF68B

P698

Q35096739-E4C90D15-CFE5-4A04-BD80-C1F35F0C0AAD

P932

Q35096739-C09A3F58-F650-4934-AF01-FE9B56E5A075

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

The reverse turn as a polypeptide conformation in globular proteins.

@en

P2093

Crawford JL

http://www.w3.org/2001/XMLSchema#string

Lipscomb WN

http://www.w3.org/2001/XMLSchema#string

Schellman CG

http://www.w3.org/2001/XMLSchema#string

P2860

Atomic coordinates for subtilisin BPN' (or Novo)

The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A

Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units

X-ray analysis and the structure of insulin.

Folding of polypeptide chains in proteins: a proposed mechanism for folding.

Carboxypeptidase A: a protein and an enzyme.

The structure of cytochrome b 5 at 2.0 Angstrom resolution.

On the conformation of the hen egg-white lysozyme molecule.

P304

538-542

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.70.2.538

http://www.w3.org/2001/XMLSchema#string

P407

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

70

http://www.w3.org/2001/XMLSchema#string

P577

1973-02-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

18656357

http://www.w3.org/2001/XMLSchema#string

P698

4510294

http://www.w3.org/2001/XMLSchema#string

P932

433301

http://www.w3.org/2001/XMLSchema#string