Structural hot spots for the solubility of globular proteins.
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Solubis: a webserver to reduce protein aggregation through mutationFusion to Flaviviral Leader Peptide Targets HIV-1 Reverse Transcriptase for Secretion and Reduces Its Enzymatic Activity and Ability to Induce Oxidative Stress but Has No Major Effects on Its Immunogenic Performance in DNA-Immunized Mice.Prediction and interpretation of deleterious coding variants in terms of protein structural stability.Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis.Computational analysis of the amino acid interactions that promote or decrease protein solubility
P2860
Structural hot spots for the solubility of globular proteins.
description
2016 nî lūn-bûn
@nan
2016 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
Structural hot spots for the solubility of globular proteins.
@ast
Structural hot spots for the solubility of globular proteins.
@en
type
label
Structural hot spots for the solubility of globular proteins.
@ast
Structural hot spots for the solubility of globular proteins.
@en
prefLabel
Structural hot spots for the solubility of globular proteins.
@ast
Structural hot spots for the solubility of globular proteins.
@en
P2093
P2860
P50
P356
P1476
Structural hot spots for the solubility of globular proteins.
@en
P2093
Aleksandra Siekierska
Ashok Ganesan
Chris Ulens
Frederic Rousseau
Greet De Baets
Hannah Wilkinson
Jacinte Beerten
Joost Van Durme
Marijke Brams
Meine Ramakers
P2860
P2888
P356
10.1038/NCOMMS10816
P407
P577
2016-02-24T00:00:00Z
P5875
P6179
1045705394