Water-Soluble Polypeptides with Elongated, Charged Side Chains Adopt Ultra-Stable Helical Conformations - Wikidata - awgldk - TriplyDB

Water-Soluble Polypeptides with Elongated, Charged Side Chains Adopt Ultra-Stable Helical Conformations

Water-Soluble Polypeptides with Elongated, Charged Side Chains Adopt Ultra-Stable Helical Conformations

http://www.wikidata.org/entity/Q38869249

about

Water-soluble poly(L-serine)s with elongated and charged side-chains: synthesis, conformations, and cell-penetrating properties A rationally designed nanoparticle for RNA interference therapy in B-lineage lymphoid malignancies Thermoresponsive and Mechanical Properties of Poly(L-proline) Gels.Stimuli-sensitive synthetic polypeptide-based materials for drug and gene delivery.Recent advances in amino acid N-carboxyanhydrides and synthetic polypeptides: chemistry, self-assembly and biological applications.Ionic α-helical polypeptides toward nonviral gene delivery.PEG-Polypeptide Dual Brush Block Copolymers: Synthesis and Application in Nanoparticle Surface PEGylation.The importance of being kinked: role of Pro residues in the selectivity of the helical antimicrobial peptide P5.Dynamic covalent polypeptides showing tunable secondary structures and thermoresponsiveness Effects of molecular weight on thermal responsive property of pegylated poly-l-glutamates Influence of the secondary structure on the AIE-related emission behavior of an amphiphilic polypeptide containing a hydrophobic fluorescent terminal and hydrophilic pendant groups

P2860

Q34361575-8D7E520B-A33C-433C-AC53-532B24BA1F89 Q34939490-BAD01370-4453-4A85-8B78-5A8B18BBE1CE Q36563797-99128E3D-FE57-436D-86CD-44DAB38E1EA2 Q38062891-E253FD74-8ACB-442E-A819-4FCB1E911A56 Q38161791-4F03CD53-9088-4C57-80FD-D1F1247B3042 Q38265866-D50D22E6-E71E-4ACE-BCFB-FF97721C8B22 Q41911787-7D1C01BC-0E45-4EF9-920F-1435B36F9713 Q44310810-0FD827E0-C983-4AA9-B0D8-797D35FAF689 Q57352996-FE1F2C1D-D277-4601-9043-7C77E48F9F9B Q57355151-06E9F35F-B5B5-4B62-AC3B-E1B0AC2EE3E6 Q57368669-F3EBBE42-7587-4069-8C0B-132E6A062B84

P2860

Water-Soluble Polypeptides with Elongated, Charged Side Chains Adopt Ultra-Stable Helical Conformations

http://www.wikidata.org/entity/Q38869249

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Water-Soluble Polypeptides wit ...... a-Stable Helical Conformations

@en

type

label

Water-Soluble Polypeptides wit ...... a-Stable Helical Conformations

@en

prefLabel

Water-Soluble Polypeptides wit ...... a-Stable Helical Conformations

@en

P1433

Q38869249-1EE404F2-1BA5-4953-AF2E-78FC5E0002FF

P1476

Q38869249-CD55ADFE-689F-4D76-B020-C3CD5241928B

P2093

Q38869249-3085942C-39FA-43E8-8D99-CC6BE2C77E8D

Q38869249-47E5E0A8-DD56-4D66-AFCE-F24898ADB3EA

Q38869249-ABCA7A3F-83B9-4F3D-953F-FF321860A376

Q38869249-F85AB5C8-5741-411D-9473-CE6F70CA4614

P2860

Q38869249-01F7B3B5-AFAC-490D-81BB-34E488E4A246

Q38869249-0205900E-85B8-4301-9486-2FBA4B099F6B

Q38869249-0F5E87DC-FC66-4CB6-9AF6-874DBB09AC38

Q38869249-15998276-DB34-4372-9570-D8D0041A42AA

Q38869249-161855DD-770A-4A7C-9403-ED14A6485A5B

Q38869249-1C5A1477-140F-497F-964E-400F804C6FBA

Q38869249-1FF3B16B-BEC5-408A-AB3F-E4E302674CE2

Q38869249-221DD064-132D-4E6A-8E5D-51E8AF222F3B

Q38869249-268CBD90-31EB-44CD-8966-A80616314C5D

Q38869249-361C5669-25E7-40D7-B2F1-1176AB832C0E

P304

Q38869249-A87D6811-7AFF-4F81-A66A-491BF34575B8

P31

Q38869249-99C97131-182C-41D8-B2B4-C91F891E1032

P356

Q38869249-08F835DA-05E4-4F1C-A241-8F07987CEB75

P433

Q38869249-ECF63A13-CBFA-4F0B-9CB4-FEE98826B63C

P478

Q38869249-A408AC9D-6AB7-4B93-897B-C77AC245B815

P577

Q38869249-C2E3FF0F-4C9C-46C0-95ED-64FB135D8D68

P5875

Q38869249-E254FD09-39CE-4C3F-9B71-531828757F39

P698

Q38869249-BA98EADB-AC29-4689-BEF2-4F24606F7C5A

P932

Q38869249-85A26D33-4E10-4ED0-AE63-81838A040C9B

P356

P1433

P1476

Water-Soluble Polypeptides wit ...... a-Stable Helical Conformations

@en

P2093

Hua Lu

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

Jianjun Cheng

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

Yanfeng Zhang

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

Yao Lin

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

P2860

Protein folding and misfolding

Dominant forces in protein folding

De novo design of helical bundles as models for understanding protein folding and function.

Metal clips that induce unstructured pentapeptides to be alpha-helical in water.

Protein design: a hierarchic approach.

"Schizophrenic" micellization associated with coil-to-helix transitions based on polypeptide hybrid double hydrophilic rod-coil diblock copolymer.

Inhibiting HIV fusion with a beta-peptide foldamer.

Unusually stable helix formation in short alanine-based peptides

Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.

Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index

P304

6641-6644

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

P31

scholarly article

P356

10.1021/MA201678R

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

P433

17

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

P478

44

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

P577

2011-09-01T00:00:00Z

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

P5875

51766226

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

P698

22049249

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

P932

3204311

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