Fast helix formation in the B domain of protein A revealed by site-specific infrared probes. - Wikidata - awgldk - TriplyDB

Fast helix formation in the B domain of protein A revealed by site-specific infrared probes.

Fast helix formation in the B domain of protein A revealed by site-specific infrared probes.

http://www.wikidata.org/entity/Q35168239

about

Efficient Total Chemical Synthesis of (13) C=(18) O Isotopomers of Human Insulin for Isotope-Edited FTIR.Mapping fast protein folding with multiple-site fluorescent probes Sequence, structure, and cooperativity in folding of elementary protein structural motifs.Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.Observation of α-Helical Hydrogen-Bond Cooperativity in an Intact Protein.Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on α-Helical Stability and Folding Kinetics A molecular engineering toolbox for the structural biologist.Simultaneous Determination of Two Subdomain Folding Rates Using the "Transfer-Quench" Method.

P2860

Q30382998-54C9CD1C-A39F-45DB-8F43-61B8F9FA4EC5 Q35818750-EDAACA82-1A73-4AE3-A6FF-2859D159DEDC Q35961459-5B0AD8A6-9B84-4708-9B81-85A39120AE5F Q37013963-B0B32C94-713E-4FEF-A5D8-7FFA6133B401 Q41554344-1AE9141D-C166-4B0C-B673-EBBE36082886 Q41812654-3D016525-B2F2-43FA-A73E-40FC60ED07E0 Q47256792-0B363F53-16EB-4A0F-8B78-368D73B1510C Q47849935-BC7D5A55-733D-4548-BB40-6F16A70B794F

P2860

Fast helix formation in the B domain of protein A revealed by site-specific infrared probes.

http://www.wikidata.org/entity/Q35168239

description

2015 nî lūn-bûn

@nan

2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Fast helix formation in the B ...... site-specific infrared probes.

@ast

Fast helix formation in the B ...... site-specific infrared probes.

@en

type

label

Fast helix formation in the B ...... site-specific infrared probes.

@ast

Fast helix formation in the B ...... site-specific infrared probes.

@en

prefLabel

Fast helix formation in the B ...... site-specific infrared probes.

@ast

Fast helix formation in the B ...... site-specific infrared probes.

@en

P1433

Q35168239-E3B9F2E6-060B-4F89-86EE-1CBCE85D4342

P1476

Q35168239-9ADC3832-6050-4C8D-9D05-F096E9B8D717

P2093

Q35168239-78003BCB-204A-4AFB-AA8B-C2A2F83D5756

Q35168239-B7848D31-7EEC-4801-AAE1-4DFA9099DEDE

Q35168239-DA04FE33-84AD-4B59-93D5-6D6458102882

P2860

Q35168239-041BE035-FA3D-4B77-AB6D-FC7045414451

Q35168239-1136772E-E2BE-4B75-B76B-C6E5E5AA0DBD

Q35168239-1D707010-C2EC-4A81-B404-AF1EE6B64DEC

Q35168239-2AB9462E-E4AB-433B-8464-7E811716C090

Q35168239-2B6766E1-6AD5-498F-9B06-1B9BC2F9FC5B

Q35168239-2B8FF8CF-67C5-4202-9EA2-696E5FA0503A

Q35168239-2FA34661-04BE-4F0C-96E8-2DC673C57C9E

Q35168239-39541876-3C62-4147-A280-1348F5AF2DDB

Q35168239-4075797D-9233-429A-A5D0-D0C216F33D0A

Q35168239-4639E5E3-C4FB-4D0E-8F6F-8AFC99F6369B

P304

Q35168239-793B4753-D608-49E3-B7F5-99C793DF1739

P31

Q35168239-B5571564-E6C6-4894-816E-B4D558DA487C

P356

Q35168239-6B9AF33A-25A3-4210-B573-5B35F6200A7D

P407

Q35168239-A9ECE1FD-4ECA-42CB-B006-8D65021917F9

P433

Q35168239-EFF5C7A4-0ADE-47F6-AD14-00B602846F4A

P478

Q35168239-40FC2F41-A964-46C4-96CE-3ACFE440DEDB

P577

Q35168239-19E7A6C1-1CC6-4808-9E89-58885E3BB1D1

P698

Q35168239-EE695547-0758-40DD-8777-7907079AF892

P932

Q35168239-12473EF6-E13A-4C67-AF37-AB658B67938D

P356

ACS.BIOCHEM.5B00037

P1433

P1476

Fast helix formation in the B ...... site-specific infrared probes.

@en

P2093

A Kat Cooper

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

Caitlin M Davis

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

R Brian Dyer

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

P2860

Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsec

Staphylococcal protein A: unfolding pathways, unfolded states, and differences between the B and E domains

What vibrations tell us about proteins.

Monte Carlo simulations of protein folding. II. Application to protein A, ROP, and crambin.

Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.

Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein.

Experimental resolution of early steps in protein folding: testing molecular dynamics simulations.

Folding a protein in a computer: an atomic description of the folding/unfolding of protein A.

Testing protein-folding simulations by experiment: B domain of protein A.

An atomically detailed study of the folding pathways of protein A with the stochastic difference equation

P304

1758-1766

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

P31

scholarly article

P356

10.1021/ACS.BIOCHEM.5B00037

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

P407

P433

9

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

P478

54

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

P577

2015-02-27T00:00:00Z

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

P698

25706439

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

P932

4356530

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