LK peptide side chain dynamics at interfaces are independent of secondary structure.

about

LK peptide side chain dynamics at interfaces are independent of secondary structure.

Item

http://www.wikidata.org/entity/Q47636203

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

LK peptide side chain dynamics at interfaces are independent of secondary structure.

@en

LK peptide side chain dynamics at interfaces are independent of secondary structure.

@nl

type

Item

label

LK peptide side chain dynamics at interfaces are independent of secondary structure.

@en

LK peptide side chain dynamics at interfaces are independent of secondary structure.

@nl

prefLabel

LK peptide side chain dynamics at interfaces are independent of secondary structure.

@en

LK peptide side chain dynamics at interfaces are independent of secondary structure.

@nl

P1476

LK peptide side chain dynamics at interfaces are independent of secondary structure.

@en

P2093

Jim Pfaendtner

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

Michael A Donovan

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

Mischa Bonn

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

Yeneneh Y Yimer

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

P2860

Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

What vibrations tell us about proteins.

Native State Volume Fluctuations in Proteins as a Mechanism for Dynamic Allostery.

Amide or amine: determining the origin of the 3300 cm(-1) NH mode in protein SFG spectra using 15N isotope labels

Protein dynamics. Direct observation of hierarchical protein dynamics.

Ultrafast Reorientational Dynamics of Leucine at the Air-Water Interface.

Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.

Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex.

Alpha-helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy.

P304

28507-28511

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

P31

scholarly article

P356

10.1039/C7CP05897G

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

P407

English

P433

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

P478

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

P50

Tobias Weidner

Helmut Lutz

P577

2017-10-18T00:00:00Z

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

P698

29043310

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