Amino acid contacts in proteins adapted to different temperatures: hydrophobic interactions and surface charges play a key role
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Medicine,General Medicine,Microbiology
Link
http://link.springer.com/content/pdf/10.1007/s00792-008-0192-4.pdf
Reference39 articles.
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3. Benson DA, Karsch-Mizrachi I et al (2000) GenBank. Nucleic Acids Res 28(1):15–18
4. Berezovsky I, Zeldovich K et al (2007) Positive and negative design in stability and thermal adaptation of natural proteins. PLoS Comput Biol 3(3):e52
5. Berman HM, Westbrook J et al (2000) The protein data bank. Nucleic Acids Res 28(1):235–242
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