Ultrafast Vibrational Dynamics of the Myoglobin Amide I Band

Peterson, Kent D.; Rella, Chris W.; Engholm, J.R.; Schwettman, H. A.

doi:10.1021/jp982398f

Cited by 76 publications

(58 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…T 1 1.5 AE 0.2 ps at 0 8 and 1.3 AE 0.2 ps at 808, respectively (data not shown). Hence, as has been noted before [24] [29] [30], T 1 relaxation of amide-I modes appears to be an intrinsic property of the peptide unit, and is not significantly affected by the local chemical structure (e.g., the amino acid residue or the difference between a-and bpeptides), the secondary structure, the solvent, the temperature [31], or the extent of delocalization.…”

supporting

confidence: 61%

On the Thermal Stability of -Peptides: A Two-Dimensional Vibrational Spectroscopy Study

Hamm

Woutersen

Rueping³

2002

HCA

View full text Add to dashboard Cite

Professor Dieter Seebach in Bewunderung und mit den besten W¸nschen zum 65. Geburtstag gewidmet.A temperature-dependent 2D-IR study of the amide-I band of a b-peptide forming a 12/10/12/10 helix is presented. Cross-relaxation of a spectrally separated marker amide-I mode, which could be assigned with the help of the NMR structure of the molecule, can be used as measure of conformational flexibility of the molecule. We find that the conformational flexibility of the N-terminal part of the helix increases slightly upon increasing the temperature from 08 to 808. The cross-peaks in the 2D-IR spectrum, and hence the connectivity of the corresponding peptide units, do not change, suggesting that the N-terminal part of the helix remains essentially intact at 808. This conclusion is in agreement with previous NMR and CD measurements.Introduction. ± Protein folding is the process of transferring information from one dimension into three dimensions, where the information that determines the molecular structure of a protein is encoded in its amino acid sequence. Understanding the mechanism by which the amino acid sequence of a protein folds into its unique native conformation is one of the biggest challenges in biophysical chemistry.The major degrees of freedom of the polypeptide chain are two s-bonds in each amino acid, which can freely rotate. The amide group (i.e., ÀCOÀNHÀ ) itself is close to planar since the CÀN bond has partial double-bond character. The free-energy surface of the two-dimensional configuration space of each amino acid has been extensively studied. A complicated balance of different forces results in two main local free-energy minima, which are of almost equal depth. Because of the large dimensionality of the problem in polypeptides and proteins, and because of the

show abstract

supporting

confidence: 61%

On the Thermal Stability of -Peptides: A Two-Dimensional Vibrational Spectroscopy Study

Hamm

Woutersen

Rueping³

2002

HCA

View full text Add to dashboard Cite

show abstract

“…41 The lifetime of CO ͑Ϸ30 ps͒ changes by less than 20% in a large temperature interval from 310 to 10 K. Also the vibrational lifetimes of the OH vibration in ice 42 as well as the amide I ͑C=O͒ vibrations of the backbone in peptides and proteins have been shown to be largely temperature independent. 43 Our observation of essentially temperature independent relaxation rates of HONO in solid Kr is in accordance with these studies.…”

Section: Discussionsupporting

confidence: 92%

Temperature dependence of the IR driven cis-trans isomerization of nitrous acid (HONO)

Botan

Hamm

2008

The Journal of Chemical Physics

View full text Add to dashboard Cite

Temperature dependence of the IR driven cis-trans isomerization of nitrous acid (HONO)Botan, V; Hamm, P Hamm, P (2008). Temperature dependence of the IR driven cis-trans isomerization of nitrous acid (HONO) AbstractWith the help of ultrafast time-resolved infrared spectroscopy, we investigate the temperature dependence of the IR driven cis->trans isomerization of nitrous acid (HONO) in solid Kr. We find that the lifetime of the OH-stretch vibration, as well as the final cooling into the matrix, is affected only minimally (if at all) by temperature. Nevertheless, the quantum yield of the cis-> trans isomerization reaction increases by approximate to 30% to a total of 50%-70% when lowering the temperature from 30 to 15 K, whereas the trans->cis back yield is reduced by approximate to 40%. The results are discussed in analogy to Marcus theory of nonadiabatic electron transfer for the essentially barrierless case. We present a unified view of this important prototype proton transfer reaction that can explain the high cis->trans quantum yield of close to one. With the help of ultrafast time-resolved infrared spectroscopy, we investigate the temperature dependence of the IR driven cis → trans isomerization of nitrous acid ͑HONO͒ in solid Kr. We find that the lifetime of the OH-stretch vibration, as well as the final cooling into the matrix, is affected only minimally ͑if at all͒ by temperature. Nevertheless, the quantum yield of the cis → trans isomerization reaction increases by Ϸ30% to a total of 50%-70% when lowering the temperature from 30 to 15 K, whereas the trans → cis back yield is reduced by Ϸ40%. The results are discussed in analogy to Marcus theory of nonadiabatic electron transfer for the essentially barrierless case. We present a unified view of this important prototype proton transfer reaction that can explain the high cis → trans quantum yield of close to 1. Temperature dependence of the IR driven cis-trans isomerization of nitrous acid "HONO…

show abstract

“…The exchange mechanism of vibrational energy within proteins is little understood. Several time‐resolved experiments were performed with picosecond and femtosecond infrared pulses to study the dissipation of locally deposited energy in the protein backbone (amide I mode) 102–104. The amide I vibrational mode involves mainly the C=O stretching motion of the peptide backbone under a small amount of mixing with the CN and NH motions 105.…”

Section: Vibrational Energy Relaxation71mentioning

confidence: 99%

Ultrafast dynamics of myoglobin probed by time‐resolved resonance Raman spectroscopy

Mizutani

Kitagawa

2001

The Chemical Record

View full text Add to dashboard Cite

Recent experimental work carried out in this laboratory on the ultrafast dynamics of myoglobin (Mb) is summarized with a stress on structural and vibrational energy relaxation. Studies on the structural relaxation of Mb following CO photolysis revealed that the structural change of heme itself, caused by CO photodissociation, is completed within the instrumental response time of the time-resolved resonance Raman apparatus used (approximately 2 ps). In contrast, changes in the intensity and frequency of the iron-histidine (Fe-His) stretching mode upon dissociation of the trans ligand were found to occur in the picosecond regime. The Fe-His band is absent for the CO-bound form, and its appearance upon photodissociation was not instantaneous, in contrast with that observed in the vibrational modes of heme, suggesting appreciable time evolution of the Fe displacement from the heme plane. The band position of the Fe-His stretching mode changed with a time constant of about 100 ps, indicating that tertiary structural changes of the protein occurred in a 100-ps range. Temporal changes of the anti-Stokes Raman intensity of the v4 and v7 bands demonstrated immediate generation of vibrationally excited heme upon the photodissociation and decay of the excited populations, whose time constants were 1.1 +/- 0.6 and 1.9 +/- 0.6 ps, respectively. In addition, the development of the time-resolved resonance Raman apparatus and prospects in this research field are described.

show abstract

Ultrafast Vibrational Dynamics of the Myoglobin Amide I Band

Cited by 76 publications

References 13 publications

On the Thermal Stability of -Peptides: A Two-Dimensional Vibrational Spectroscopy Study

On the Thermal Stability of -Peptides: A Two-Dimensional Vibrational Spectroscopy Study

Temperature dependence of the IR driven cis-trans isomerization of nitrous acid (HONO)

Ultrafast dynamics of myoglobin probed by time‐resolved resonance Raman spectroscopy

Contact Info

Product

Resources

About