CORE
🇺🇦
make metadata, not war
Services
Services overview
Explore all CORE services
Access to raw data
API
Dataset
FastSync
Content discovery
Recommender
Discovery
OAI identifiers
OAI Resolver
Managing content
Dashboard
Bespoke contracts
Consultancy services
Support us
Support us
Membership
Sponsorship
Community governance
Advisory Board
Board of supporters
Research network
About
About us
Our mission
Team
Blog
FAQs
Contact us
A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity
Authors
Khadiullina A.
Sirotkin V.
Publication date
1 January 2014
Publisher
Abstract
The excess volumes of the binary system of ribonuclease A (RNase A) with water were obtained as a function of composition at 25 °C. The excess quantities for RNase A were compared with the published data for several unrelated proteins (lysozyme, serum albumin, lactoglobulin, and chymotrypsinogen A). The hydrophobicity of these proteins is gradually changed over a wide range. It was found that the more hydrophilic a protein is, the more significant the hydrophilic hydration contribution is. RNase A is the most hydrophilic protein in the present study, and it has the most significant hydrophilic hydration contribution. © 2014 Elsevier B.V. All rights reserved
Similar works
Full text
Open in the Core reader
Download PDF
Available Versions
Kazan Federal University Digital Repository
See this paper in CORE
Go to the repository landing page
Download from data provider
oai:dspace.kpfu.ru:net/136008
Last time updated on 07/05/2019