Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pH.
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Observation of the closing of individual hydrogen bonds during TFE-induced helix formation in a peptideSubmillisecond folding of monomeric lambda repressorBoth the fast and slow refolding reactions of ribonuclease A yield native enzyme.The stability of globular proteins.Thermal unfolding of ribonuclease A in phosphate at neutral pH: deviations from the two-state model.A Fourier transform NMR study of the thermal denaturation of ribonuclease A at low pH.Effect of molecular crowding on the temperature-pressure stability diagram of ribonuclease AHigh Temperature Electrophoresis for Monitoring the Thermal Behavior of Cytochrome b5
P2860
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P2860
Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pH.
description
1973 nî lūn-bûn
@nan
1973 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1973 թվականի մարտին հրատարակված գիտական հոդված
@hy
1973年の論文
@ja
1973年論文
@yue
1973年論文
@zh-hant
1973年論文
@zh-hk
1973年論文
@zh-mo
1973年論文
@zh-tw
1973年论文
@wuu
name
Nuclear magnetic resonance stu ...... multistate behavior at low pH.
@ast
Nuclear magnetic resonance stu ...... multistate behavior at low pH.
@en
type
label
Nuclear magnetic resonance stu ...... multistate behavior at low pH.
@ast
Nuclear magnetic resonance stu ...... multistate behavior at low pH.
@en
prefLabel
Nuclear magnetic resonance stu ...... multistate behavior at low pH.
@ast
Nuclear magnetic resonance stu ...... multistate behavior at low pH.
@en
P2860
P356
P1476
Nuclear magnetic resonance stu ...... multistate behavior at low pH.
@en
P2093
Matthews CR
Westmoreland DG
P2860
P304
P356
10.1073/PNAS.70.3.914
P407
P577
1973-03-01T00:00:00Z