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1 the lowest, pK=0.6, is observed for Asp76 in ribonuclease T1.
2 red helix propensities in the alpha-helix of ribonuclease T1 and a helical peptide of identical seque
3  on temperature of the unfolding enthalpy of ribonuclease T1 and the solvation enthalpies of the nonp
4 trictocin homologues, non-structure-specific ribonucleases T1 and U2.
5 ids for an alpha-helix in an intact protein, ribonuclease T1, and for a 17-residue peptide with a seq
6              Our helix propensities based on ribonuclease T1 are in good agreement with those from si
7    This agreement suggests that the helix of ribonuclease T1 behaves as an independently stabilized s
8      We examined the thermal denaturation of ribonuclease T1 by CD using both the original and expand
9 les were analyzed by coupling an immobilized ribonuclease T1 cartridge to a hydrophilic interaction l
10 nst an alpha-helix, seen in the well-studied ribonuclease T1 despite a lack of sequence similarity.
11 ndence of helix assembly measured by partial ribonuclease T1 digestion and of an unfolding transition
12 eotides also is recognized as guanine during ribonuclease T1 digestion.
13 w folding of circularly permuted variants of ribonuclease T1 has been examined using steady-state and
14 c residues at the C terminus of the helix of ribonuclease T1 have recently been reported.
15 e and the reversible thermal denaturation of ribonuclease T1 in H2O.
16 e, we investigated the refolding reaction of ribonuclease T1 in the presence of the prolyl isomerase
17               At pH 7, the stability of D76A ribonuclease T1 is 3.8 kcal mol(-1) less than wild-type,
18           Helix propensities measured in the ribonuclease T1 peptide/protein are compared with those
19         The side-chain carboxyl of Asp 76 in ribonuclease T1 (RNase T1) is buried, charged, non-ion-p
20 he HL mutant was less helical near the IL/B (ribonuclease T1 sensitive) and less stable (T(m) decreas
21 xposure in the native and unfolded states of ribonuclease T1, the transfer free energies of native an
22                   At lower concentrations of ribonuclease T1, two regions of partial protection are s
23                       Partial digestion with ribonuclease T1 under identical conditions showed that t
24                                              Ribonuclease T1 was the only enzyme that preserved ribos
25 tein substrates, dihydrofolate reductase and ribonuclease T1, whose folding is accelerated by prolyl