2002
DOI: 10.1016/s0022-2836(02)00137-7
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NMR Studies of the Backbone Flexibility and Structure of Human Growth Hormone: A Comparison of High and Low pH Conformations

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Cited by 35 publications
(56 citation statements)
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References 48 publications
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“…As such, structural characterisation of the synthetic isoform was approached through CD and limited proteolysis experiments. CD provided a global insight of the total secondary structure of the protein and showed a partial helicoidal structure of the 5 kDa isoform in agreement with the conformation shown on the AA 1 -43 sequence within the 22 kDa structure (Kasimova et al 2002). The addition of TFE to the media resulted in a fast increment of the a-helix content revealing a low resistance of the rest of the protein to adopt a folded state, synonym of a notable grade of flexibility within the chain.…”
Section: Synthesis and Structure Of 5 Kda Gh Isoformsupporting
confidence: 66%
See 1 more Smart Citation
“…As such, structural characterisation of the synthetic isoform was approached through CD and limited proteolysis experiments. CD provided a global insight of the total secondary structure of the protein and showed a partial helicoidal structure of the 5 kDa isoform in agreement with the conformation shown on the AA 1 -43 sequence within the 22 kDa structure (Kasimova et al 2002). The addition of TFE to the media resulted in a fast increment of the a-helix content revealing a low resistance of the rest of the protein to adopt a folded state, synonym of a notable grade of flexibility within the chain.…”
Section: Synthesis and Structure Of 5 Kda Gh Isoformsupporting
confidence: 66%
“…This constitutes a modification in the structure of the AA 1 -43 sequence in comparison when it is included into the AA 1 -191 22 kDa sequence. Within the latter, the 5 kDa fragment conforms the first helix of the 22 kDa protein (Kasimova et al 2002), having therefore the central part of the 5 kDa sequence structured in an helicoidal state. The C-terminal part of the 5 kDa sequence is known to constitute part of the first minihelix of the 22 kDa isoform, but it has been observed that such mini-helix might not be present in the 22 kDa free isoform, i.e.…”
Section: Synthesis and Structure Of 5 Kda Gh Isoformmentioning
confidence: 99%
“…This built-in structural plasticity of hGH in this particular structural segment has been documented by several studies pointing to high flexibility in this area. 27,49 This flexibility may not be present in PL or PRL. We suggest that this mini-helix forms the basis for the promiscuity of hGH in its receptor interaction preferences.…”
Section: Binding Sitementioning
confidence: 99%
“…The highly evolved interface of wt-hGH appears to have been "primed" for recognition, such that the 15-residues substitution in hGHv does not affect the free energy to reach the transition state. Even in its aciddestabilized state as surveyed by NMR, wt-hGH displays dramatically increased dynamics, yet still retains its secondary conformations (29), which may be attributed to the 4-helix bundle topology. Second, destabilization in the unbound hGHbp may also play an important role.…”
Section: (I) What Happened To the Binding Hot-spot?mentioning
confidence: 99%