Dynamics of tropomyosin in muscle fibers as monitored by saturation transfer EPR of bi-functional probe. - Wikidata - awgldk - TriplyDB

Dynamics of tropomyosin in muscle fibers as monitored by saturation transfer EPR of bi-functional probe.

Dynamics of tropomyosin in muscle fibers as monitored by saturation transfer EPR of bi-functional probe.

http://www.wikidata.org/entity/Q33941983

about

Full Atom Simulations of Spin Label Conformations Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.The use of the Rx spin label in orientation measurement on proteins, by EPR.Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain Technological advances in site-directed spin labeling of proteins.Tropomyosin dynamics.Overview of the Muscle Cytoskeleton.Calcium-dependent interaction sites of tropomyosin on reconstituted muscle thin filaments with bound Myosin heads as studied by site-directed spin-labeling.

P2860

Q27334941-584D4166-D2F3-477F-8F76-B6CF76A54BE5 Q35239853-55D9658F-C83C-44A6-910C-607CCC72BB95 Q36587544-00EAAB5A-5CF9-4C2B-8BC5-66E41BB36EED Q37624251-199911FA-D187-402F-A687-B359ABB7AB4C Q38121297-99A0C5D8-C8D8-4AF0-879C-CF6D20B1E0C8 Q38186601-D2AA94A4-2D89-49DF-B818-A61A7A60DF37 Q39391006-2B169643-C023-4EA5-A285-E6BF9A98E56D Q42183103-CA125526-B7EE-4342-8117-59A123A9DF48

P2860

Dynamics of tropomyosin in muscle fibers as monitored by saturation transfer EPR of bi-functional probe.

http://www.wikidata.org/entity/Q33941983

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

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

name

Dynamics of tropomyosin in mus ...... er EPR of bi-functional probe.

@ast

Dynamics of tropomyosin in mus ...... er EPR of bi-functional probe.

@en

type

label

Dynamics of tropomyosin in mus ...... er EPR of bi-functional probe.

@ast

Dynamics of tropomyosin in mus ...... er EPR of bi-functional probe.

@en

prefLabel

Dynamics of tropomyosin in mus ...... er EPR of bi-functional probe.

@ast

Dynamics of tropomyosin in mus ...... er EPR of bi-functional probe.

@en

P1433

Q33941983-DB5AF4A8-D17C-4965-B342-8CA51F67D93D

P1476

Q33941983-06B1393A-6481-45DB-9DD6-E1687B33B427

P2093

Q33941983-29F2D975-BF07-4ABF-8D90-A3F620F3B7D5

Q33941983-690FAA9C-EB02-4BBA-A6ED-420E118524BF

Q33941983-820564D2-0012-4489-BA5F-0C5C8B835797

Q33941983-9F4C87E6-776E-44F4-B788-FA87C0A2F20B

P2860

Q33941983-0345B2B6-B8C7-4A86-85D8-1847CF2BE388

Q33941983-0787E4BA-DA7D-465B-A1D0-075A2A608D2E

Q33941983-081C934B-EDF7-4478-AB8A-88A2B2EFC86F

Q33941983-1120D3F8-8F7F-46B0-A037-716734123635

Q33941983-14051CE9-A412-47E8-992F-7939A255AFB9

Q33941983-16D36BD6-601D-4341-BC6A-FA6531EC800E

Q33941983-35457EDF-D0A5-48C0-8F99-BED9BF290406

Q33941983-405FFBA4-6D8D-4CE4-BEC3-ED63656A725C

Q33941983-4C8AB50C-C459-4712-9FD7-B5D7C523559D

Q33941983-4F90FA59-78B4-4CD2-9336-1DCB48EE592F

P304

Q33941983-66EB20F6-93E4-482B-A1D2-26DE4A1A522D

P31

Q33941983-5D45A214-7615-4C29-B569-A5E0DADB0FF9

P356

Q33941983-46868858-6446-400E-B07E-5803A8240265

P407

Q33941983-87168A45-6FCC-4CAD-8145-225566AF8799

P433

Q33941983-583F04A1-4600-4143-B200-674088E0CF00

P478

Q33941983-15EE2B69-83B3-463B-AE4B-1A53EF2EAAA6

P50

Q33941983-B9173656-F919-4D67-AB78-60E04E75DD77

P577

Q33941983-D2E337C5-37F2-4E53-808E-0A6307C229DE

P5875

Q33941983-D6405ED0-6CA5-43B1-BCA4-019431F1ECAD

P698

Q33941983-AD6394B0-E380-4066-9435-5C3F6746D655

P932

Q33941983-DEB4EA03-8C88-4C2F-9EF4-19545997A957

P356

JOURNAL.PONE.0021277

P1433

P1476

Dynamics of tropomyosin in mus ...... fer EPR of bi-functional probe

@en

P2093

Kálmán Hideg

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

Piotr G Fajer

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

Roni F Rayes

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

Tamás Kálai

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

P2860

Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament

The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin

Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics.

Baseline length and automated fitting of denaturation data.

Rotational dynamics of spin-labeled F-actin during activation of myosin S1 ATPase using caged ATP

Resolving Conformational and Rotameric Exchange in Spin-Labeled Proteins Using Saturation Recovery EPR

The relationship between curvature, flexibility and persistence length in the tropomyosin coiled-coil

Diffuse x-ray scattering from tropomyosin crystals

Tropomyosin positions in regulated thin filaments revealed by cryoelectron microscopy.

Structure and interactions of the carboxyl terminus of striated muscle alpha-tropomyosin: it is important to be flexible.

P304

e21277

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

P31

scholarly article

P356

10.1371/JOURNAL.PONE.0021277

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

P407

P433

6

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

P478

6

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

P50

Michael A. Geeves

P577

2011-06-20T00:00:00Z

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

P5875

51246336

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

P698

21701580

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

P932

3118794

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