Glucosylation of beta-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics - Wikidata - wikimedia - TriplyDB

Glucosylation of beta-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics

Glucosylation of beta-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics

http://www.wikidata.org/entity/Q30350967

about

The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin Insight into the glycation of milk proteins: an ESI- and MALDI-MS perspective (review).Effects of glycosylation on the stability of protein pharmaceuticals.Functional Stability of HIV-1 Envelope Trimer Affects Accessibility to Broadly Neutralizing Antibodies at its Apex.Digestibility and IgE-binding of glycosylated codfish parvalbumin.Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5.Effect of quality of milk on maillard reaction and protein oxidation during preparation of cow and buffalo milk khoa.

P2860

Q27654616-3E2B25AB-A52F-4A6E-A069-11FB98D6FE4A Q33872386-0AF70F1B-AC21-48C3-8FDD-A88BDF3A4D79 Q37114305-E49B5B4C-F340-4038-9C9B-8300A63CA5F9 Q41924154-E4498E29-CC9F-4CD5-92AC-FBB479FF3812 Q42151397-52140963-00DC-4CED-BF9C-393DD7AA781D Q42243126-E2C4956A-571D-4A3F-9B23-F924F42D7E68 Q47775346-9DC7B2A4-9028-4469-A0DC-BA80BD14D8D6

P2860

Glucosylation of beta-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics

http://www.wikidata.org/entity/Q30350967

description

2005 nî lūn-bûn

@nan

2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Glucosylation of beta-lactoglo ...... affect protein thermodynamics

@ast

Glucosylation of beta-lactoglo ...... affect protein thermodynamics

@en

type

label

Glucosylation of beta-lactoglo ...... affect protein thermodynamics

@ast

Glucosylation of beta-lactoglo ...... affect protein thermodynamics

@en

prefLabel

Glucosylation of beta-lactoglo ...... affect protein thermodynamics

@ast

Glucosylation of beta-lactoglo ...... affect protein thermodynamics

@en

P1433

Q30350967-23DD1A43-35EC-430E-8DAA-B6DBD996632F

P1476

Q30350967-6B5FFB53-5380-4C59-BFD8-7D589EC72FBB

P2093

Q30350967-25D35E13-621B-4411-B8C7-C98719DA6545

Q30350967-7FC71DA2-067A-499B-BC9E-B83162CE0923

Q30350967-FFE59E1C-6E1C-4DFD-95B5-B1CF210BD3F9

P2860

Q30350967-004E13CC-EF64-4E6B-886A-B66E883FBD66

Q30350967-01BCC552-FE6A-49ED-8B04-ACB7DAC8126C

Q30350967-059C204E-1280-40CB-8FB1-7845DD58FE8C

Q30350967-0C792959-14C4-457C-8D34-28F40236D67E

Q30350967-2A8707F5-5F74-4DD4-8AA3-D7FF11A3059E

Q30350967-416461DB-0287-4C1C-BC4A-D7C5429A9279

Q30350967-42842ABF-8E54-40DC-81F3-553E10D4BA8E

Q30350967-4310C1B9-0D2B-480B-8601-81DE0F4F0E2D

Q30350967-680C585B-5EBA-44B9-9616-50475602D23A

Q30350967-859764B0-7FF5-4E49-89EE-4E33032872F0

P304

Q30350967-C5D9DE1F-074D-4A96-9402-43B1D6F944AE

P31

Q30350967-24CF7A0D-BFA0-4D7F-B713-75758B46A7DC

P356

Q30350967-DE114E3C-8D85-4725-A82D-CCC403AD9F53

P433

Q30350967-2C6EC5DF-5AD8-4FCC-83CE-93D3D3ED2FE1

P478

Q30350967-55B86D41-8345-41E8-A6D8-44927E548F1C

P577

Q30350967-E17D5163-5096-481F-B425-2F86FDBFA7C2

P5875

Q30350967-B83BF758-530D-459F-BC99-51CA6B1B6FAB

P698

Q30350967-89BCDF94-C325-435C-A3DB-72297A465E41

P932

Q30350967-56E755B4-E4B6-4240-8B90-5A145E40AC64

P356

P1433

Protein Science

P1476

Glucosylation of beta-lactoglo ...... affect protein thermodynamics

@en

P2093

Annemarie M M van Teeffelen

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

Harmen H J de Jongh

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

Kerensa Broersen

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

P2860

Two exposed amino acid residues confer thermostability on a cold shock protein

Determination and analysis of urea and guanidine hydrochloride denaturation curves

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

Heat-induced aggregation of recombinant erythropoietin in the intact and deglycosylated states as monitored by gel permeation chromatography combined with a low-angle laser light scattering technique.

To charge or not to charge?

Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.

Increasing protein stability by altering long-range coulombic interactions.

Some thermodynamic implications for the thermostability of proteins.

The preparation and characterization of some Amadori compounds (1-amino-1-deoxy-D-fructose derivatives) derived from a series of aliphatic omega-amino acids.

Diabetic cataract formation: potential role of glycosylation of lens crystallins.

P304

2187-2194

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

P31

scholarly article

P356

10.1110/PS.051405005

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

P433

8

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

P478

14

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

P577

2005-06-29T00:00:00Z

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

P5875

7755904

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

P698

15987887

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

P932

2279330

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