Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa
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Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsSolution Structure of Calmodulin Bound to the Binding Domain of the HIV-1 Matrix ProteinCharge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.Peptide sequence and conformation strongly influence tryptophan fluorescence.Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.Structural basis to characterise transactivation domain of BRCA1
P2860
Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa
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2004 nî lūn-bûn
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2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
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2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2004年の論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年论文
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name
Contribution of single tryptop ...... d stability of ribonuclease Sa
@ast
Contribution of single tryptop ...... d stability of ribonuclease Sa
@en
Contribution of single tryptop ...... d stability of ribonuclease Sa
@nl
type
label
Contribution of single tryptop ...... d stability of ribonuclease Sa
@ast
Contribution of single tryptop ...... d stability of ribonuclease Sa
@en
Contribution of single tryptop ...... d stability of ribonuclease Sa
@nl
prefLabel
Contribution of single tryptop ...... d stability of ribonuclease Sa
@ast
Contribution of single tryptop ...... d stability of ribonuclease Sa
@en
Contribution of single tryptop ...... d stability of ribonuclease Sa
@nl
P2093
P2860
P1433
P1476
Contribution of single tryptop ...... d stability of ribonuclease Sa
@en
P2093
C Nick Pace
Gregory D Reinhart
J Martin Scholtz
Jozef Sevcik
Mauricio Lasagna
Roy W Alston
P2860
P304
P356
10.1529/BIOPHYSJ.104.050377
P407
P50
P577
2004-09-17T00:00:00Z