Selection of side-chain carbons in a high-molecular-weight, hydrophobic peptide using solid-state spectral editing methods.
about
Solid-state (13)C NMR reveals effects of temperature and hydration on elastin(13)C cross-polarization/magic angle spinning NMR studies of alpha-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links.Cooperativity between the hydrophobic and cross-linking domains of elastin
P2860
Selection of side-chain carbons in a high-molecular-weight, hydrophobic peptide using solid-state spectral editing methods.
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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name
Selection of side-chain carbon ...... tate spectral editing methods.
@en
Selection of side-chain carbon ...... tate spectral editing methods.
@nl
type
label
Selection of side-chain carbon ...... tate spectral editing methods.
@en
Selection of side-chain carbon ...... tate spectral editing methods.
@nl
prefLabel
Selection of side-chain carbon ...... tate spectral editing methods.
@en
Selection of side-chain carbon ...... tate spectral editing methods.
@nl
P2093
P356
P1476
Selection of side-chain carbon ...... tate spectral editing methods.
@en
P2093
K K Kumashir
L B Sandberg
W P Niemczura
P2888
P304
P356
10.1023/A:1008334931234
P577
2000-10-01T00:00:00Z
P6179
1035580130