about
On the satisfaction of backbone-carbonyl lone pairs of electrons in protein structures.A Single Stereodynamic Center Modulates the Rate of Self-Assembly in a Biomolecular System.n→π* Interactions Are Competitive with Hydrogen Bonds.Forces stabilizing proteinsMolecular recognition in chemical and biological systems.Crystal structure of N-(3-oxo-butano-yl)-l-homoserine lactone.Unconventional N-H…N Hydrogen Bonds Involving Proline Backbone Nitrogen in Protein Structures.4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins.Reciprocal carbonyl-carbonyl interactions in small molecules and proteins.The n→π* InteractionProtein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.n→π* interactions engender chirality in carbonyl groupsA key n→π* Interaction in N-acyl homoserine lactones.Attractive Interactions between Heteroallenes and the Cucurbituril Portal.pH-Responsive Aminoproline-Containing Collagen Triple Helices.
P2860
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P2860
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年学术文章
@wuu
2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
@yue
2014年學術文章
@zh
2014年學術文章
@zh-hant
name
Signatures of n→π* interactions in proteins.
@en
Signatures of n→π* interactions in proteins.
@nl
type
label
Signatures of n→π* interactions in proteins.
@en
Signatures of n→π* interactions in proteins.
@nl
prefLabel
Signatures of n→π* interactions in proteins.
@en
Signatures of n→π* interactions in proteins.
@nl
P2860
P50
P356
P1433
P1476
Signatures of n→π* interactions in proteins
@en
P2093
Brett VanVeller
Gail J Bartlett
P2860
P304
P356
10.1002/PRO.2413
P577
2014-03-01T00:00:00Z