thermostability

Known as: thermolability 
 
National Institutes of Health

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Review
2001
Review
2001
With the advent of directed evolution techniques, protein engineering has received a fresh impetus. Engineering proteins for… (More)
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Highly Cited
2001
Highly Cited
2001
A common mutation in methylenetetrahydrofolate reductase (MTHFR), 677C-->T, is associated with reduced enzyme activity, a… (More)
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Highly Cited
2000
Highly Cited
2000
Thermophilic organisms produce proteins of exceptional stability. To understand protein thermostability at the molecular level we… (More)
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Review
1999
Review
1999
Homocysteine is a sulfur amino acid whose metabolism stands at the intersection of two pathways: remethylation to methionine… (More)
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Highly Cited
1999
Highly Cited
1999
Understanding the molecular determinants of protein thermostability is of theoretical and practical importance. While numerous… (More)
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Highly Cited
1999
Highly Cited
1999
Understanding the role of various interactions in enhancing the thermostability of proteins is important not only for clarifying… (More)
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Highly Cited
1999
Highly Cited
1999
Reduction of 5,10-methylenetetrahydrofolate (methyleneTHF), a donor for methylating dUMP to dTMP in DNA synthesis, to 5… (More)
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Highly Cited
1995
Highly Cited
1995
Hyperhomocysteinaemia has been identified as a risk factor for cerebrovascular, peripheral vascular and coronary heart disease1–4… (More)
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Highly Cited
1987
Highly Cited
1987
Thermostability of proteins arises from the simultaneous effect of several forces, which in fact lead to decreased flexibility of… (More)
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Highly Cited
1952
Highly Cited
1952
Different strains of staphylococci vary in ability to produce free coagulase. Methods are given for the selection of suitable… (More)
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